protein

This hashtag in English

Last updated 18w.

Proteins are large biomolecules and macromolecules that are comprised of one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity.

A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides, or sometimes oligopeptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residues in a protein is defined by the sequence of a gene, which is encoded in the genetic code. In general, the genetic code specifies 20 standard amino acids; but in certain organisms the genetic code can include selenocysteine and—in certain archaeapyrrolysine. Shortly after or even during synthesis, the residues in a protein are often chemically modified by post-translational modification, which alters the physical and chemical properties, folding, stability, activity, and ultimately, the function of the proteins. Some proteins have non-peptide groups attached, which can be called prosthetic groups or cofactors. Proteins can also work together to achieve a particular function, and they often associate to form stable protein complexes.

Once formed, proteins only exist for a certain period and are then degraded and recycled by the cell's machinery through the process of protein turnover. A protein's lifespan is measured in terms of its half-life and covers a wide range. They can exist for minutes or years with an average lifespan of 1–2 days in mammalian cells. Abnormal or misfolded proteins are degraded more rapidly either due to being targeted for destruction or due to being unstable.

Like other biological macromolecules such as polysaccharides and nucleic acids, proteins are essential parts of organisms and participate in virtually every process within cells. Many proteins are enzymes that catalyse biochemical reactions and are vital to metabolism. Proteins also have structural or mechanical functions, such as actin and myosin in muscle and the proteins in the cytoskeleton, which form a system of scaffolding that maintains cell shape. Other proteins are important in cell signaling, immune responses, cell adhesion, and the cell cycle. In animals, proteins are needed in the diet to provide the essential amino acids that cannot be synthesized. Digestion breaks the proteins down for use in the metabolism.

Proteins may be purified from other cellular components using a variety of techniques such as ultracentrifugation, precipitation, electrophoresis, and chromatography; the advent of genetic engineering has made possible a number of methods to facilitate purification. Methods commonly used to study protein structure and function include immunohistochemistry, site-directed mutagenesis, X-ray crystallography, nuclear magnetic resonance and mass spectrometry.

Proteins were recognized as a distinct class of biological molecules in the eighteenth century by Antoine Fourcroy and others, distinguished by the molecules' ability to coagulate or flocculate under treatments with heat or acid. Noted examples at the time included albumin from egg whites, blood serum albumin, fibrin, and wheat gluten.

Proteins were first described by the Dutch chemist Gerardus Johannes Mulder and named by the Swedish chemist Jöns Jacob Berzelius in 1838. Mulder carried out elemental analysis of common proteins and found that nearly all proteins had the same empirical formula, C400H620N100O120P1S1. He came to the erroneous conclusion that they might be composed of a single type of (very large) molecule. The term "protein" to describe these molecules was proposed by Mulder's associate Berzelius; protein is derived from the Greek word πρώτειος (proteios), meaning "primary", "in the lead", or "standing in front", + -in. Mulder went on to identify the products of protein degradation such as the amino acid leucine for which he found a (nearly correct) molecular weight of 131 Da. Prior to "protein", other names were used, like "albumins" or "albuminous materials" (Eiweisskörper, in German).

Early nutritional scientists such as the German Carl von Voit believed that protein was the most important nutrient for maintaining the structure of the body, because it was generally believed that "flesh makes flesh." Karl Heinrich Ritthausen extended known protein forms with the identification of glutamic acid. At the Connecticut Agricultural Experiment Station a detailed review of the vegetable proteins was compiled by Thomas Burr Osborne. Working with Lafayette Mendel and applying Liebig's law of the minimum in feeding laboratory rats, the nutritionally essential amino acids were established. The work was continued and communicated by William Cumming Rose. The understanding of proteins as polypeptides came through the work of Franz Hofmeister and Hermann Emil Fischer in 1902. The central role of proteins as enzymes in living organisms was not fully appreciated until 1926, when James B. Sumner showed that the enzyme urease was in fact a protein.

The difficulty in purifying proteins in large quantities made them very difficult for early protein biochemists to study. Hence, early studies focused on proteins that could be purified in large quantities, e.g., those of blood, egg white, various toxins, and digestive/metabolic enzymes obtained from slaughterhouses. In the 1950s, the Armour Hot Dog Co. purified 1 kg of pure bovine pancreatic ribonuclease A and made it freely available to scientists; this gesture helped ribonuclease A become a major target for biochemical study for the following decades.

Linus Pauling is credited with the successful prediction of regular protein secondary structures based on hydrogen bonding, an idea first put forth by William Astbury in 1933. Later work by Walter Kauzmann on denaturation, based partly on previous studies by Kaj Linderstrøm-Lang, contributed an understanding of protein folding and structure mediated by hydrophobic interactions.

The first protein to be sequenced was insulin, by Frederick Sanger, in 1949. Sanger correctly determined the amino acid sequence of insulin, thus conclusively demonstrating that proteins consisted of linear polymers of amino acids rather than branched chains, colloids, or cyclols. He won the Nobel Prize for this achievement in 1958.

The first protein structures to be solved were hemoglobin and myoglobin, by Max Perutz and Sir John Cowdery Kendrew, respectively, in 1958. As of 2017, the Protein Data Bank has over 126,060 atomic-resolution structures of proteins. In more recent times, cryo-electron microscopy of large macromolecular assemblies and computational protein structure prediction of small protein domains are two methods approaching atomic resolution.

The number of proteins encoded in a genome roughly corresponds to the number of genes (although there may be a significant number of genes that encode RNA of protein, e.g. ribosomal RNAs). Viruses typically encode a few to a few hundred proteins, archaea and bacteria a few hundred to a few thousand, while eukaryotes typically encode a few thousand up to tens of thousands of proteins (see genome size for a list of examples).

Most proteins consist of linear polymers built from series of up to 20 different L-α- amino acids. All proteinogenic amino acids possess common structural features, including an α-carbon to which an amino group, a carboxyl group, and a variable side chain are bonded. Only proline differs from this basic structure as it contains an unusual ring to the N-end amine group, which forces the CO–NH amide moiety into a fixed conformation. The side chains of the standard amino acids, detailed in the list of standard amino acids, have a great variety of chemical structures and properties; it is the combined effect of all of the amino acid side chains in a protein that ultimately determines its three-dimensional structure and its chemical reactivity. The amino acids in a polypeptide chain are linked by peptide bonds. Once linked in the protein chain, an individual amino acid is called a residue, and the linked series of carbon, nitrogen, and oxygen atoms are known as the main chain or protein backbone.:19

The peptide bond has two resonance forms that contribute some double-bond character and inhibit rotation around its axis, so that the alpha carbons are roughly coplanar. The other two dihedral angles in the peptide bond determine the local shape assumed by the protein backbone.:31 The end with a free amino group is known as the N-terminus or amino terminus, whereas the end of the protein with a free carboxyl group is known as the C-terminus or carboxy terminus (the sequence of the protein is written from N-terminus to C-terminus, from left to right).

The words protein, polypeptide, and peptide are a little ambiguous and can overlap in meaning. Protein is generally used to refer to the complete biological molecule in a stable conformation, whereas peptide is generally reserved for a short amino acid oligomers often lacking a stable 3D structure. But the boundary between the two is not well defined and usually lies near 20–30 residues. Polypeptide can refer to any single linear chain of amino acids, usually regardless of length, but often implies an absence of a defined conformation.

Proteins can interact with many types of molecules, including with other proteins, with lipids, with carboyhydrates, and with DNA.

It has been estimated that average-sized bacteria contain about 2 million proteins per cell (e.g. E. coli and Staphylococcus aureus). Smaller bacteria, such as Mycoplasma or spirochetes contain fewer molecules, on the order of 50,000 to 1 million. By contrast, eukaryotic cells are larger and thus contain much more protein. For instance, yeast cells have been estimated to contain about 50 million proteins and human cells on the order of 1 to 3 billion. The concentration of individual protein copies ranges from a few molecules per cell up to 20 million. Not all genes coding proteins are expressed in most cells and their number depends on, for example, cell type and external stimuli. For instance, of the 20,000 or so proteins encoded by the human genome, only 6,000 are detected in lymphoblastoid cells.

Proteins are assembled from amino acids using information encoded in genes. Each protein has its own unique amino acid sequence that is specified by the nucleotide sequence of the gene encoding this protein. The genetic code is a set of three-nucleotide sets called codons and each three-nucleotide combination designates an amino acid, for example AUG (adenineuracilguanine) is the code for methionine. Because DNA contains four nucleotides, the total number of possible codons is 64; hence, there is some redundancy in the genetic code, with some amino acids specified by more than one codon.:1002–42 Genes encoded in DNA are first transcribed into pre-messenger RNA (mRNA) by proteins such as RNA polymerase. Most organisms then process the pre-mRNA (also known as a primary transcript) using various forms of Post-transcriptional modification to form the mature mRNA, which is then used as a template for protein synthesis by the ribosome. In prokaryotes the mRNA may either be used as soon as it is produced, or be bound by a ribosome after having moved away from the nucleoid. In contrast, eukaryotes make mRNA in the cell nucleus and then translocate it across the nuclear membrane into the cytoplasm, where protein synthesis then takes place. The rate of protein synthesis is higher in prokaryotes than eukaryotes and can reach up to 20 amino acids per second.

The process of synthesizing a protein from an mRNA template is known as translation. The mRNA is loaded onto the ribosome and is read three nucleotides at a time by matching each codon to its base pairing anticodon located on a transfer RNA molecule, which carries the amino acid corresponding to the codon it recognizes. The enzyme aminoacyl tRNA synthetase "charges" the tRNA molecules with the correct amino acids. The growing polypeptide is often termed the nascent chain. Proteins are always biosynthesized from N-terminus to C-terminus.:1002–42

The size of a synthesized protein can be measured by the number of amino acids it contains and by its total molecular mass, which is normally reported in units of daltons (synonymous with atomic mass units), or the derivative unit kilodalton (kDa). The average size of a protein increases from Archaea to Bacteria to Eukaryote (283, 311, 438 residues and 31, 34, 49 kDa respectively) due to a bigger number of protein domains constituting proteins in higher organisms. For instance, yeast proteins are on average 466 amino acids long and 53 kDa in mass. The largest known proteins are the titins, a component of the muscle sarcomere, with a molecular mass of almost 3,000 kDa and a total length of almost 27,000 amino acids.

Short proteins can also be synthesized chemically by a family of methods known as peptide synthesis, which rely on organic synthesis techniques such as chemical ligation to produce peptides in high yield. Chemical synthesis allows for the introduction of non-natural amino acids into polypeptide chains, such as attachment of fluorescent probes to amino acid side chains. These methods are useful in laboratory biochemistry and cell biology, though generally not for commercial applications. Chemical synthesis is inefficient for polypeptides longer than about 300 amino acids, and the synthesized proteins may not readily assume their native tertiary structure. Most chemical synthesis methods proceed from C-terminus to N-terminus, opposite the biological reaction.

Most proteins fold into unique 3D structures. The shape into which a protein naturally folds is known as its native conformation.:36 Although many proteins can fold unassisted, simply through the chemical properties of their amino acids, others require the aid of molecular chaperones to fold into their native states.:37 Biochemists often refer to four distinct aspects of a protein's structure::30–34

Proteins are not entirely rigid molecules. In addition to these levels of structure, proteins may shift between several related structures while they perform their functions. In the context of these functional rearrangements, these tertiary or quaternary structures are usually referred to as "conformations", and transitions between them are called conformational changes. Such changes are often induced by the binding of a substrate molecule to an enzyme's active site, or the physical region of the protein that participates in chemical catalysis. In solution proteins also undergo variation in structure through thermal vibration and the collision with other molecules.:368–75

Proteins can be informally divided into three main classes, which correlate with typical tertiary structures: globular proteins, fibrous proteins, and membrane proteins. Almost all globular proteins are soluble and many are enzymes. Fibrous proteins are often structural, such as collagen, the major component of connective tissue, or keratin, the protein component of hair and nails. Membrane proteins often serve as receptors or provide channels for polar or charged molecules to pass through the cell membrane.:165–85

A special case of intramolecular hydrogen bonds within proteins, poorly shielded from water attack and hence promoting their own dehydration, are called dehydrons.

Many proteins are composed of several protein domains, i.e. segments of a protein that fold into distinct structural units. Domains usually also have specific functions, such as enzymatic activities (e.g. kinase) or they serve as binding modules (e.g. the SH3 domain binds to proline-rich sequences in other proteins).

Short amino acid sequences within proteins often act as recognition sites for other proteins. For instance, SH3 domains typically bind to short PxxP motifs (i.e. 2 prolines [P], separated by two unspecified amino acids [x], although the surrounding amino acids may determine the exact binding specificity). Many such motifs has been collected in the Eukaryotic Linear Motif (ELM) database.

Proteins are the chief actors within the cell, said to be carrying out the duties specified by the information encoded in genes. With the exception of certain types of RNA, most other biological molecules are relatively inert elements upon which proteins act. Proteins make up half the dry weight of an Escherichia coli cell, whereas other macromolecules such as DNA and RNA make up only 3% and 20%, respectively. The set of proteins expressed in a particular cell or cell type is known as its proteome.

The chief characteristic of proteins that also allows their diverse set of functions is their ability to bind other molecules specifically and tightly. The region of the protein responsible for binding another molecule is known as the binding site and is often a depression or "pocket" on the molecular surface. This binding ability is mediated by the tertiary structure of the protein, which defines the binding site pocket, and by the chemical properties of the surrounding amino acids' side chains. Protein binding can be extraordinarily tight and specific; for example, the ribonuclease inhibitor protein binds to human angiogenin with a sub-femtomolar dissociation constant (<10−15 M) but does not bind at all to its amphibian homolog onconase (>1 M). Extremely minor chemical changes such as the addition of a single methyl group to a binding partner can sometimes suffice to nearly eliminate binding; for example, the aminoacyl tRNA synthetase specific to the amino acid valine discriminates against the very similar side chain of the amino acid isoleucine.

Proteins can bind to other proteins as well as to small-molecule substrates. When proteins bind specifically to other copies of the same molecule, they can oligomerize to form fibrils; this process occurs often in structural proteins that consist of globular monomers that self-associate to form rigid fibers. Protein–protein interactions also regulate enzymatic activity, control progression through the cell cycle, and allow the assembly of large protein complexes that carry out many closely related reactions with a common biological function. Proteins can also bind to, or even be integrated into, cell membranes. The ability of binding partners to induce conformational changes in proteins allows the construction of enormously complex signaling networks.:830–49 As interactions between proteins are reversible, and depend heavily on the availability of different groups of partner proteins to form aggregates that are capable to carry out discrete sets of function, study of the interactions between specific proteins is a key to understand important aspects of cellular function, and ultimately the properties that distinguish particular cell types.

The best-known role of proteins in the cell is as enzymes, which catalyse chemical reactions. Enzymes are usually highly specific and accelerate only one or a few chemical reactions. Enzymes carry out most of the reactions involved in metabolism, as well as manipulating DNA in processes such as DNA replication, DNA repair, and transcription. Some enzymes act on other proteins to add or remove chemical groups in a process known as posttranslational modification. About 4,000 reactions are known to be catalysed by enzymes. The rate acceleration conferred by enzymatic catalysis is often enormous—as much as 1017-fold increase in rate over the uncatalysed reaction in the case of orotate decarboxylase (78 million years without the enzyme, 18 milliseconds with the enzyme).

The molecules bound and acted upon by enzymes are called substrates. Although enzymes can consist of hundreds of amino acids, it is usually only a small fraction of the residues that come in contact with the substrate, and an even smaller fraction—three to four residues on average—that are directly involved in catalysis. The region of the enzyme that binds the substrate and contains the catalytic residues is known as the active site.

Dirigent proteins are members of a class of proteins that dictate the stereochemistry of a compound synthesized by other enzymes.

Many proteins are involved in the process of cell signaling and signal transduction. Some proteins, such as insulin, are extracellular proteins that transmit a signal from the cell in which they were synthesized to other cells in distant tissues. Others are membrane proteins that act as receptors whose main function is to bind a signaling molecule and induce a biochemical response in the cell. Many receptors have a binding site exposed on the cell surface and an effector domain within the cell, which may have enzymatic activity or may undergo a conformational change detected by other proteins within the cell.:251–81

Antibodies are protein components of an adaptive immune system whose main function is to bind antigens, or foreign substances in the body, and target them for destruction. Antibodies can be secreted into the extracellular environment or anchored in the membranes of specialized B cells known as plasma cells. Whereas enzymes are limited in their binding affinity for their substrates by the necessity of conducting their reaction, antibodies have no such constraints. An antibody's binding affinity to its target is extraordinarily high.:275–50

Many ligand transport proteins bind particular small biomolecules and transport them to other locations in the body of a multicellular organism. These proteins must have a high binding affinity when their ligand is present in high concentrations, but must also release the ligand when it is present at low concentrations in the target tissues. The canonical example of a ligand-binding protein is haemoglobin, which transports oxygen from the lungs to other organs and tissues in all vertebrates and has close homologs in every biological kingdom.:222–29 Lectins are sugar-binding proteins which are highly specific for their sugar moieties. Lectins typically play a role in biological recognition phenomena involving cells and proteins. Receptors and hormones are highly specific binding proteins.

Transmembrane proteins can also serve as ligand transport proteins that alter the permeability of the cell membrane to small molecules and ions. The membrane alone has a hydrophobic core through which polar or charged molecules cannot diffuse. Membrane proteins contain internal channels that allow such molecules to enter and exit the cell. Many ion channel proteins are specialized to select for only a particular ion; for example, potassium and sodium channels often discriminate for only one of the two ions.:232–34

Structural proteins confer stiffness and rigidity to otherwise-fluid biological components. Most structural proteins are fibrous proteins; for example, collagen and elastin are critical components of connective tissue such as cartilage, and keratin is found in hard or filamentous structures such as hair, nails, feathers, hooves, and some animal shells.:178–81 Some globular proteins can also play structural functions, for example, actin and tubulin are globular and soluble as monomers, but polymerize to form long, stiff fibers that make up the cytoskeleton, which allows the cell to maintain its shape and size.

Other proteins that serve structural functions are motor proteins such as myosin, kinesin, and dynein, which are capable of generating mechanical forces. These proteins are crucial for cellular motility of single celled organisms and the sperm of many multicellular organisms which reproduce sexually. They also generate the forces exerted by contracting muscles:258–64, 272 and play essential roles in intracellular transport.

A key question in molecular biology is how proteins evolve, i.e. how can mutations (or rather changes in amino acid sequence) lead to new structures and functions? Most amino acids in a protein can be changed without disrupting activity or function, as can be seen from numerous homologous proteins across species (as collected in specialized databases for protein families, e.g. PFAM). In order to prevent dramatic consequences of mutations, a gene may be duplicated before it can mutate freely. However, this can also lead to complete loss of gene function and thus pseudo-genes. More commonly, single amino acid changes have limited consequences although some can change protein function substantially, especially in enzymes. For instance, many enzymes can change their substrate specificity by one or a few mutations. Changes in substrate specificity are facilitated by substrate promiscuity, i.e. the ability of many enzymes to bind and process multiple substrates. When mutations occur, the specificity of an enzyme can increase (or decrease) and thus its enzymatic activity. Thus, bacteria (or other organisms) can adapt to different food sources, including unnatural substrates such as plastic.

The activities and structures of proteins may be examined in vitro, in vivo, and in silico. In vitro studies of purified proteins in controlled environments are useful for learning how a protein carries out its function: for example, enzyme kinetics studies explore the chemical mechanism of an enzyme's catalytic activity and its relative affinity for various possible substrate molecules. By contrast, in vivo experiments can provide information about the physiological role of a protein in the context of a cell or even a whole organism. In silico studies use computational methods to study proteins.

To perform in vitro analysis, a protein must be purified away from other cellular components. This process usually begins with cell lysis, in which a cell's membrane is disrupted and its internal contents released into a solution known as a crude lysate. The resulting mixture can be purified using ultracentrifugation, which fractionates the various cellular components into fractions containing soluble proteins; membrane lipids and proteins; cellular organelles, and nucleic acids. Precipitation by a method known as salting out can concentrate the proteins from this lysate. Various types of chromatography are then used to isolate the protein or proteins of interest based on properties such as molecular weight, net charge and binding affinity.:21–24 The level of purification can be monitored using various types of gel electrophoresis if the desired protein's molecular weight and isoelectric point are known, by spectroscopy if the protein has distinguishable spectroscopic features, or by enzyme assays if the protein has enzymatic activity. Additionally, proteins can be isolated according to their charge using electrofocusing.

For natural proteins, a series of purification steps may be necessary to obtain protein sufficiently pure for laboratory applications. To simplify this process, genetic engineering is often used to add chemical features to proteins that make them easier to purify without affecting their structure or activity. Here, a "tag" consisting of a specific amino acid sequence, often a series of histidine residues (a "His-tag"), is attached to one terminus of the protein. As a result, when the lysate is passed over a chromatography column containing nickel, the histidine residues ligate the nickel and attach to the column while the untagged components of the lysate pass unimpeded. A number of different tags have been developed to help researchers purify specific proteins from complex mixtures.

The study of proteins in vivo is often concerned with the synthesis and localization of the protein within the cell. Although many intracellular proteins are synthesized in the cytoplasm and membrane-bound or secreted proteins in the endoplasmic reticulum, the specifics of how proteins are targeted to specific organelles or cellular structures is often unclear. A useful technique for assessing cellular localization uses genetic engineering to express in a cell a fusion protein or chimera consisting of the natural protein of interest linked to a "reporter" such as green fluorescent protein (GFP). The fused protein's position within the cell can be cleanly and efficiently visualized using microscopy, as shown in the figure opposite.

Other methods for elucidating the cellular location of proteins requires the use of known compartmental markers for regions such as the ER, the Golgi, lysosomes or vacuoles, mitochondria, chloroplasts, plasma membrane, etc. With the use of fluorescently tagged versions of these markers or of antibodies to known markers, it becomes much simpler to identify the localization of a protein of interest. For example, indirect immunofluorescence will allow for fluorescence colocalization and demonstration of location. Fluorescent dyes are used to label cellular compartments for a similar purpose.

Other possibilities exist, as well. For example, immunohistochemistry usually utilizes an antibody to one or more proteins of interest that are conjugated to enzymes yielding either luminescent or chromogenic signals that can be compared between samples, allowing for localization information. Another applicable technique is cofractionation in sucrose (or other material) gradients using isopycnic centrifugation. While this technique does not prove colocalization of a compartment of known density and the protein of interest, it does increase the likelihood, and is more amenable to large-scale studies.

Finally, the gold-standard method of cellular localization is immunoelectron microscopy. This technique also uses an antibody to the protein of interest, along with classical electron microscopy techniques. The sample is prepared for normal electron microscopic examination, and then treated with an antibody to the protein of interest that is conjugated to an extremely electro-dense material, usually gold. This allows for the localization of both ultrastructural details as well as the protein of interest.

Through another genetic engineering application known as site-directed mutagenesis, researchers can alter the protein sequence and hence its structure, cellular localization, and susceptibility to regulation. This technique even allows the incorporation of unnatural amino acids into proteins, using modified tRNAs, and may allow the rational design of new proteins with novel properties.

The total complement of proteins present at a time in a cell or cell type is known as its proteome, and the study of such large-scale data sets defines the field of proteomics, named by analogy to the related field of genomics. Key experimental techniques in proteomics include 2D electrophoresis, which allows the separation of many proteins, mass spectrometry, which allows rapid high-throughput identification of proteins and sequencing of peptides (most often after in-gel digestion), protein microarrays, which allow the detection of the relative levels of the various proteins present in a cell, and two-hybrid screening, which allows the systematic exploration of protein–protein interactions. The total complement of biologically possible such interactions is known as the interactome. A systematic attempt to determine the structures of proteins representing every possible fold is known as structural genomics.

Discovering the tertiary structure of a protein, or the quaternary structure of its complexes, can provide important clues about how the protein performs its function and how it can be affected, i.e. in drug design. As proteins are too small to be seen under a light microscope, other methods have to be employed to determine their structure. Common experimental methods include X-ray crystallography and NMR spectroscopy, both of which can produce structural information at atomic resolution. However, NMR experiments are able to provide information from which a subset of distances between pairs of atoms can be estimated, and the final possible conformations for a protein are determined by solving a distance geometry problem. Dual polarisation interferometry is a quantitative analytical method for measuring the overall protein conformation and conformational changes due to interactions or other stimulus. Circular dichroism is another laboratory technique for determining internal β-sheet / α-helical composition of proteins. Cryoelectron microscopy is used to produce lower-resolution structural information about very large protein complexes, including assembled viruses;:340–41 a variant known as electron crystallography can also produce high-resolution information in some cases, especially for two-dimensional crystals of membrane proteins. Solved structures are usually deposited in the Protein Data Bank (PDB), a freely available resource from which structural data about thousands of proteins can be obtained in the form of Cartesian coordinates for each atom in the protein.

Many more gene sequences are known than protein structures. Further, the set of solved structures is biased toward proteins that can be easily subjected to the conditions required in X-ray crystallography, one of the major structure determination methods. In particular, globular proteins are comparatively easy to crystallize in preparation for X-ray crystallography. Membrane proteins and large protein complexes, by contrast, are difficult to crystallize and are underrepresented in the PDB. Structural genomics initiatives have attempted to remedy these deficiencies by systematically solving representative structures of major fold classes. Protein structure prediction methods attempt to provide a means of generating a plausible structure for proteins whose structures have not been experimentally determined.

Complementary to the field of structural genomics, protein structure prediction develops efficient mathematical models of proteins to computationally predict the molecular formations in theory, instead of detecting structures with laboratory observation. The most successful type of structure prediction, known as homology modeling, relies on the existence of a "template" structure with sequence similarity to the protein being modeled; structural genomics' goal is to provide sufficient representation in solved structures to model most of those that remain. Although producing accurate models remains a challenge when only distantly related template structures are available, it has been suggested that sequence alignment is the bottleneck in this process, as quite accurate models can be produced if a "perfect" sequence alignment is known. Many structure prediction methods have served to inform the emerging field of protein engineering, in which novel protein folds have already been designed. Also proteins (in eukaryotes ~33%) contain large unstructured but biologically functional segments and can be classified as intrinsically disordered proteins. Predicting and analysing protein disorder is, therefore, an important part of protein structure characterisation.

A vast array of computational methods have been developed to analyze the structure, function and evolution of proteins. The development of such tools has been driven by the large amount of genomic and proteomic data available for a variety of organisms, including the human genome. It is simply impossible to study all proteins experimentally, hence only a few are subjected to laboratory experiments while computational tools are used to extrapolate to similar proteins. Such homologous proteins can be efficiently identified in distantly related organisms by sequence alignment. Genome and gene sequences can be searched by a variety of tools for certain properties. Sequence profiling tools can find restriction enzyme sites, open reading frames in nucleotide sequences, and predict secondary structures. Phylogenetic trees can be constructed and evolutionary hypotheses developed using special software like ClustalW regarding the ancestry of modern organisms and the genes they express. The field of bioinformatics is now indispensable for the analysis of genes and proteins.

A more complex computational problem is the prediction of intermolecular interactions, such as in molecular docking, protein folding, protein–protein interaction and chemical reactivity. Mathematical models to simulate these dynamical processes involve molecular mechanics, in particular, molecular dynamics. In this regard, in silico simulations discovered the folding of small α-helical protein domains such as the villin headpiece, the HIV accessory protein and hybrid methods combining standard molecular dynamics with quantum mechanical mathematics have explored the electronic states of rhodopsins.

Beyond classical molecular dynamics, quantum dynamics methods allow the simulation of proteins in atomistic detail with an accurate description of quantum mechanical effects. Examples include the multi-layer multi-configuration time-dependent Hartree (MCTDH) method and the hierarchical equations of motion (HEOM) approach, which have been applied to plant cryptochromes and bacteria light-harvesting complexes, respectively. Both quantum and classical mechanical simulations of biological-scale systems are extremely computationally demanding, so distributed computing initiatives (for example, the Folding@home project) facilitate the molecular modeling by exploiting advances in GPU parallel processing and Monte Carlo techniques.

The total nitrogen content of organic matter is mainly formed by the amino groups in proteins. The Total Kjeldahl Nitrogen (TKN) is a measure of nitrogen widely used in the analysis of (waste) water, soil, food, feed and organic matter in general. As the name suggests, the Kjeldahl method is applied. More sensitive methods are available.

Most microorganisms and plants can biosynthesize all 20 standard amino acids, while animals (including humans) must obtain some of the amino acids from the diet. The amino acids that an organism cannot synthesize on its own are referred to as essential amino acids. Key enzymes that synthesize certain amino acids are not present in animals—such as aspartokinase, which catalyses the first step in the synthesis of lysine, methionine, and threonine from aspartate. If amino acids are present in the environment, microorganisms can conserve energy by taking up the amino acids from their surroundings and downregulating their biosynthetic pathways.

In animals, amino acids are obtained through the consumption of foods containing protein. Ingested proteins are then broken down into amino acids through digestion, which typically involves denaturation of the protein through exposure to acid and hydrolysis by enzymes called proteases. Some ingested amino acids are used for protein biosynthesis, while others are converted to glucose through gluconeogenesis, or fed into the citric acid cycle. This use of protein as a fuel is particularly important under starvation conditions as it allows the body's own proteins to be used to support life, particularly those found in muscle.

In animals such as dogs and cats, protein maintains the health and quality of the skin by promoting hair follicle growth and keratinization, and thus reducing the likelihood of skin problems producing malodours. Poor-quality proteins also have a role regarding gastrointestinal health, increasing the potential for flatulence and odorous compounds in dogs because when proteins reach the colon in an undigested state, they are fermented producing hydrogen sulfide gas, indole, and skatole. Dogs and cats digest animal proteins better than those from plants, but products of low-quality animal origin are poorly digested, including skin, feathers, and connective tissue.

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RT @ravenscimaven: Well, let's list some you should follow: @TheSpaceGal @hood_naturalist @astronaia @SusannaLHarris @Ologies @Ehmee…
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Milk and milk products contain a good balance of protein, fat and carbohydrate and are a very important source of essential nutrients.
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RT @red3xxx: Who needs a Early morning protein shake🥛
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@Pupperchucks I’ll stick with my protein, low carb diet. I know it works 😂
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@7brkyC @demarkesports @ertansuzgun Haklısın protein tozu kardeşim. Sizin Yönetim şahane işler başardı.
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When the going gets tough there is always breakfast for dinner. @eatmagicspoon @oikos #protein #breakfastfordinner…
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A new mutation of the Kent variant detected in 11 samples could help it evade the immune system. The mutation chan…
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If Flynn had redirected all his anger about being dismissed by Obama into cross fit gyms and protein shakes instead…
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7) Also how long did anti #SARSCoV2 spike protein IgG antibody last after just a single dose? A long time- at least…
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Scientists have engineered tumor cells to secrete a protein that triggers a death switch in other tumor cells they…
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For mutations in #SARSCoV2, we've been fixated on the spike protein's receptor binding domain (RBD), S1. Just out…
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i will be damned if i ever eat protein powder dear god
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RT @djtristanjaxx: Blasting that protein all over
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RT @djtristanjaxx: Blasting that protein all over
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神引き来たぁあ! またしても10連
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RT @barbonpoblano2: El semen es la mejor proteína y el secreto para tener una barba más gruesa y abundante / Semen is the best protein and…
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RT @KamounLab: Monino-Lopez et al. Allelic variants of the NLR protein Rpi-chc1 differentially recognise members of the Phytophthora infest…
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RT @SabzerAzoh: In fact meat is not ideal for the human body. The human body is intended to function on plant-based foods that are full of…
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Congrats to all the team! || Flow cytometry multiplexed method for the detection of neutralizing human antibodies t…
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It also isn’t a protein source 16g of Fat 6g of Carbs (if you’re lucky) 8g of Protein Great for increasing calori…
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RT @J_md95: Protein Brownies, Protein Strawberry Swole Cake, and Chocolate Chip Protein Cookies! Coming back soon...
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@Karami_loveee I only drink the pre-made premier protein ones. They’re the best tasting ones to me! Chocolate, vani…
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RT @bodytreatmen: 3D animation of DNA to Protein.
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RT @TheFoodBankMO: We are grateful for our partnership with @BeyondMeat, which has donated more than 740,000 pounds of plant-based protein…
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@therealzoedoll Come on nih 😂😂 you’d be surprised.. vegans put on more weight &amp; they do it healthier at a faster rate. It’s all protein.
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@xMas0nx both! i take a whey protein pre workout, and a gainer mixed with the same whey protein post and between an…
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I am reconnecting to former pastimes. One is reading recipes. Lentils have a surprising amount of protein.…
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@CNNPolitics Oatmeal and tofu, easy to get organic, good protein and plenty of fiber.
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The hidden dangers of protein powders: #HarvardHealth
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the "chemistry of the unexpected" right now tho is when a spike protein gets hooked on your cell thingie and then 3…
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i hate tuna fish but god it’s such a good low calorie meal. 90 calories for a whole can and lots of protein with ba…
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RT @ShabekLab: Wow...fantastic work from Brenda Schulman's group: #Ubiquitin ligation to F-box protein targets by SCF–RBR E3–E3 super-assem…
1
@ShadeSolomon @StarTribune Why do soyboys with no pic always critique everyone elses' looks first instead of going…
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Peanut butter is an awesome post-cardio snack. You can put peanut butter on whole wheat crackers, graham crackers,…
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Drinking protein shake and taking pre within the same hour is a laxative bro
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RT @EmilyGorcenski: the "chemistry of the unexpected" right now tho is when a spike protein gets hooked on your cell thingie and then 3 wee…
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RT @JerzyRydzewski: Szczepionka MRNA blokuje białko, które pomaga w tworzeniu się ludzkiego łożyska ''
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RT @sailorrooscout: Looking ahead, we are expecting Oxford/AstraZeneca’s, Johnson &amp; Johnson’s, and Novavax’s Coronavirus vaccines to be aut…
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Prep hack- food storage: Yes the dehydrated stuff is great to build into your pantry for long-term use. But it’s…
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RT @tednaiman: @MichaelMindrum @garytaubes When it comes to fat loss and reversing obesity/diabetes/metabolic syndrome, the solution must,…
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Empirical Study of Protein Feature Representation on Deep Belief Networks Trained with Small Data for Secondary Str…
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RT @TechRxiv_org: Empirical Study of Protein Feature Representation on Deep Belief Networks Trained with Small Data for Secondary Structure…
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RT @JerzyRydzewski: Szczepionka MRNA blokuje białko, które pomaga w tworzeniu się ludzkiego łożyska ''
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my current drawing ability seems to be however long I draw for, I need to rest an equal amount of time. Im not sure…
0
( 카톡: oticket ) sweet 휴대폰소액결제 정책 fantastic 신용카드깡 lead 카드한도현금화 factory 신용카드현금화 meal 휴대폰정보이용료 side 핸드폰소액결제 protein 구글정보이용료 365일 24시 언제나 친절상담
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@shsternberg @stanleyqilab @joeBondyDenomy For what it's worth, the protein sequence in the supplement of the origi…
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RT @jhdavislab: O so excited our paper is out today. Amazing work in collaboration with @ZhongingAlong, @tbepler1, and @lab_berger allows u…
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SCAREMONGERS: Bread contains 'zero protein' and is 'full of gluten'!!! SCIENCE: Gluten is the protein found in wh…
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Well it's thirsty work performing all these blowjobs and I needed a protein drink 😉 -
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@FiannaFatale Fresh veggies aren’t even expensive.... if you’re buying natural high protein plant based food and no…
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RT @HodariNundu: A female Titanoboa eats a male after mating for extra protein during gestation :B Doodle inspired by sexual cannibalism re…
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@RealThebasicb Damn that's the worst. I've been on the hunt for another protein company the one I used to buy from…
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No Cow Protein Bars, Peanut Butter Chocolate Chip, 21g Plant Based Vegan Protein, Keto, Low Sugar, Low Carb, Low Ca…
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RT @mackinprof: Second, only to fat-burners (complete and total waste), BCAA are a useless supplement that provides no useful tangible bene…
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JP07:15 i found Protein cost performance No1 at local, Soy Powder 240g 100cent at Worldwide DAISO !! Protein about100g !! Protein1g1cent !!
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Peanut butter banana protein shakes are the 🐐
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Been eating a fillet of salmon or 2 chicken breasts almost daily, with brown rice. Still a fraction of my desired d…
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RT @bbcslutforeverr: My bulls @imalison4 @hot_mov1 @Cockhot1 feeding me my protein shake 🍆🍆🍆💦👄💋😋 yummy
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SlimFast Original Creamy Milk Chocolate Shake – Ready to Drink Weight Loss Meal Replacement – 10g Protein – 11 Fl.…
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RT @kiti_twi_bot: 大事な学年なので二回繰り返しました
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RT @hanaharu833: 〜健康を愛する全ての人へ。 ANOMA プロテイン 様から(@anoma_protein) 新年お年玉企画で ANOMAプロテイントライアルセットを 頂きました💪✨ ANOMAは 「世界で最も強く優しい」を コンセプトに創られた 質にこだ…
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Do you want a delicious protein bar [NuviaGo] ? Visit the below URL for details and purchase with discounted price:…
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No Cow Protein Bars, Raspberry Truffle, 21g Plant Based Vegan Protein, Keto Friendly, Low Sugar, Low Carb, Low Calo…
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@thericecakepoll I have before but I make sure to get a lot of protein in my diet and take vitamins now
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Shout out tiktok for all the protein meal ideas. 💯
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To celebrate #BlackHistoryMonth, we highlight University of Florida assistant professor Carl Denard, whose lab seek…
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The virus DOES NOT have a brain It is a lump of my protein A person infected with the UK strain will pass the vir…
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Power Protein Brownies
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We've got loads of recipes on our website for pancake showstoppers this #pancake day! Including these dreamy chocol…
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@tadkins613 @lilySerenity Tfw yr fiance waits until you start prepping dinner to eat their breakfast in the form of…
0
RT @hetaregbf:
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JP18:15 i found Protein cost performance No1 at local, Soy Powder 240g 100cent at Worldwide DAISO !! Protein about100g !! Protein1g1cent !!
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RT @NPGalerts: The Protein Works announces 40% growth. #health #wellness #nutrition #sportsnutrition #natural #nat…
1
Don't miss out. Join us on Feb 25th for our free online workshop 'N-terminal processing and proteolysis.' Places ar…
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RT @blessed_213: How about a protein shot with your coffee today? Full video showing face, dirty talk, and cum is on my onlyfans which has…
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RT @OrgyFucker: Open your mouth and eat that sperm, sluts! 🍆💦💦💦 @GreyColton’s hot piece of squirting male flesh has got some fresh protein…
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RT @tasty: Power Protein Brownies
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@desjavoo1 it’s bad when you drink too much. as too much protein can be vry bad !
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The #mutation discovered by scientists affects the work of the OCA2 gene. The protein encoded by this #gene perform…
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RT @Elwyngeen: @bully_zw @Makomborerol Protein and fat. The liver is an excellent organ. Probably the most important
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@DelilahVeronese: @LAMuscle: The Bodybuilders Cheesecake Recipe by Mr Universe Neale Cranwell here:…
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@SriSitaRamDas @BangadVedant 😂 Dont be sarcastic We indians in general consume protein deficient diet
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@Hexatiouz @hishosiness Organic raised chicken. Which means he ran around and did parkour all his life and went to…
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RT @diettipsbest: Tips lain untuk turun berat: 1. Minum air sebelum makan berat 2. Makan secara perlahan 3. Elakkan mknan manis &amp; juice bu…
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【定期】【マッスルスイーツ】#筋トレ後の「プロテインパンケーキ」レシピ → #美容
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*NEW* This high protein low carb food guide is meant to be a curated resource to support you, and help you make every meal a celebration that tastes good and is good for you! #highproteinlowcarbfoods #highproteinketofoods
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These protein meal recipes are just the very best if you're working out and trying to build muscle. If you're starting a high protein meal plan, these meal prep dishes will help you out! #mealplan #mealprep #highprotein
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If you're on a low carb diet and want to get in enough protein, try these low carb high protein snack ideas. These low carb snacks will fill you up and keep you on a high protein diet. #lowcarb #snacks
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Chocolate protein pudding is the perfect afternoon snack or healthy dessert! This low carb high protein pudding is ready in about 2 minutes and is gluten free, dairy free, vegan and so easy to make! Only 4 ingredients!
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Delicious sources of plant based vegan protein. Vegan protein sources that work perfectly in recipes, especially pancakes. These are the healthiest best plant protein sources.
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Auch Sportler wollen naschen: Dieses Rezept für Protein-Waffeln ist genau richtig, wenn du auch beim Nachtisch möglichst viel Eiweiß zu dir nehmen möchtest. Und Quark-Waffeln sind ja immer gut...#diät #kalorienarm #daskochrezept #protein #eiweiß #quark #waffel #sportler
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Protein-Pancakes
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Zum Frühstück ein paar leckere Waffeln genießen und das ganz ohne Zucker? Dieses Rezept für High Protein Waffeln macht es möglich. Der Quark macht die Waffeln superfluffig und sie kommen ganz ohne Mehl und Zucker aus. #leichtesfrühstück #proteinwaffeln #lowcarbwaffeln #lowcarbrezept #einfachbacken
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16 High Protein Snackideen – alle über 20g Eiweiß. Meine besten Rezepte für eiweißreiche Snacks. Kalorienarme Snacks für Zwischendurch, die uns aber trotzdem mit Eiweiß versorgen. #protein #snacks #abnehmen #snackideen
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Protein-Spinat-Muffins mit Feta: Schnelles, einfaches Low-Carb-Rezept für herzhafte, gesunde Muffins mit Joghurt, Frischkäse und Eiweißpulver. Die saftigen, kalorienarmen Muffins schmecken als Eiweiß-Diät-Mahlzeit, Pausen-Snack zum Mitnehmen, vegetarisches Protein-Frühstück zum Abnehmen und als kleines Mittag- oder Abendessen ...
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protein Pinterest Ideas
  • protein balls
  • protein shakes
  • protein pancakes
  • protein snacks
  • protein foods
  • protein shake recipes
  • protein powder recipes
Feb 12, 2021 09:38
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Remède anti coup de blues hivernal !!!!Une recette simple pour booster votre organisme Régalez-vous 🧡 en gardant la ligne 👍☆TAGLIATELLES DE CAROTTES VIOLETTES ☆On fait le plein d'Antioxydants et de Vitamines 💪2 carottes/personne passées à la mandoline (à défaut à l'économe) Quelques noisettes ☆VINAIGRETTE AU KAKI☆Dans votre blinder, mixez la chair d'un kaki, 3 feuilles de Verveine, 2 CS d'huile de noisettes, le jus d'1/2 citron, un tour de poivre et une pincée de sel KANJI (lien dans ma bio).BON APPÉTIT !!!#healthyfood #healthylifestyle #recette #veggie #ecofriendly #faitmaison #blogger #good #mood #food #laglaneuse #ecofriendly #slow #veggiefood #nutrition #protein
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#mood #faitmaison #healthyfood #veggie #laglaneuse
Jan 31, 2021 14:38
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@joerogan with some more inspirational messages to keep you going 💪 Double tap for more ❤❤ - Follow @fittnessdragon ❤ Follow @fittnessdragon ❤ Follow @fittnessdragon ❤ - - - #fittnessdragon #bestfitnesstipz and #fitnessgyms is #gymworkoutmotivation #protein but also #musclegaintips and #healthfood with food even #healthyfood but #macros is for #fitnessusa #gymexercise and #buildmuscleburnfat without #befitmotivation you won’t #nutrition and become #gymfitnessidol by doing #gymexercises with #gymaddiction to get we share #exercisetips and #workoutfoods and #workoutdiet even #dietfoods for #dietplanner and #dietplans creating #dietmealplan sharing #diettips helping #fitnessdiet for your #gymdiet and #gymmemes
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#gymexercise #gymdiet #befitmotivation #gymmemes #macros
Jan 31, 2021 14:37
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Minum protein hari-hari untuk kekal sihat 😊 Saralicious vitamin 0172023543 #protein #espshaklee
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#protein #espshaklee
Jan 31, 2021 14:38
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Made one of those eggy wraps and melted @eatlean protein cheese into it 🤤 . . . 484 calories / 48.6g protein . . . . . . #caloriecounting #protein #bingeeatingdisorderrecovery #tryingtoeating #eatyourgreens #makegoodchoices #bekind #bekindtoyourself #healthy #foodbloguk #weightloss #diet #dietsaretoxic #nutracheck #nutracheckapp #caloriecounting #caloriedeficit #caloriedeficitdiet #happy #weightlossjourney #selflove #bekind #weighin #weighinday #weighinsaturday #wwlife #fattofit #health #disorderedeating #disorderedeatingrecovery
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#fattofit #caloriedeficit #makegoodchoices #wwlife #weighinday
Jan 31, 2021 14:38
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#postworkout #fitness #workout #preworkout #protein #gym #fitnessmotivation #healthylifestyle #bodybuilding #nutrition #health #fit #fitfam #healthy #healthyfood #muscle #vegan #motivation #gymlife #recovery #postworkoutmeal #weightloss #crossfit #supplements #lifestyle #diet #wellness #food #bhfyp @themilan12
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#preworkout #fit #nutrition #lifestyle #muscle
Jan 31, 2021 14:38
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S T O R Y T I M E ⠀ ⠀ Ok - remember when we reopened after the break and we told everyone we were getting a really large drying cabinet? We finally got it sorted as of this weekend, not without turmoil of course. ⠀ ⠀ A true tale of ‘nothin’ ever comes easy’. Right - I head out to Mascot to pick up my this monstrosity. Good start that I forgot my tie downs. After about 2 hours I strap the Biltong cabinet down onto my ute. With the help of one of our neighbours we managed to get the cabinet in (scratched the fuck out of the walls and floors btw as well as needing to disassemble a doors) only to find the wall plug provided was 15amp (larger than normal). We were a bit disappointed but managed to get an electrician there quickly to sort it. ⠀ We then decided to load the unit up with about 25-30kgs so we could get on top of the backlog of orders we had. In they went. Everything seemed fine for the first few hours then, all of a sudden my partner and I had severely sore eyes. It was to the point where we couldn’t see, we had no idea what happened so we called the ambulance. Turns out the vapour from the chilli we used essentially pepper sprayed us 😂 we had changed chilli providers for that batch as our usual supplier didn’t have enough in stock. We both took about 48h to fully recover and I had to go back to collect some items scuba’d up lol⠀ ⠀ Onwards and upwards as they say! We’ve fixed the issue and back in business as per normal proceedings. ⠀ ⠀ As promised, we have dramatically reduced wait times for orders, with the addition of this very large drying cabinet, you shouldn’t be waiting more than a week for your order. We still make all batches to order and do not provide product that’s been sitting around waiting to be sold. Fresh is best. ⠀ ⠀ 📥 DM us with your order!⠀ ⠀ @theherd_biltong ⠀ .⠀ . ⠀ .⠀ .⠀ #beef #biltong #beefbiltong #australianbeef #jerky #beefjerky #droewors #drywors #sydneyfoodie #penrithcity #westernsydneyeats #penrith #protein #artesian #smallbatch #supportsmallbusiness #westernsydney #southafrica #southafricanfood #southafricansnacks #biltongmaker #biltonglover #healthysnack #healthyeating #nosugar⠀
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#southafrica #penrithcity #healthysnack #westernsydney #biltonglover
Jan 31, 2021 14:38
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#gym #gymmotivation #musculation #nutrition #eau #budybuilding #coach #instagram #aerobic #algerie #omega_3 #legume #protein #الماء_هو_الحياة #التغذية_الصحية #الرياضة #الماء #الحمية_العلاجية #البروتينات
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#coach #omega_3 #gymmotivation #aerobic #protein
Jan 31, 2021 14:38
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Biscoff protien fudge by the protein fudge queen the best!! @theproteinqueenofficial #myfitnesspal #mfp #caloriecounting #iifym #macrocounting #protein #fibre #caloriedeficit #instafood #weightloss #fatloss #loosingweight #maintenance #gains #flexibledieting #healthreno #caloriesincaloriesout #caloriecounter #foodblogger #foodforleisure #foodidary #foodblogger #workoutsathome #fitness #healthylifestyle #fuelyourbody #nutrition #trackmacros #foodideas #trainedbycb #courtneyblackapp
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#workoutsathome #gains #caloriecounting #protein #fibre
Jan 31, 2021 14:38
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Questa struttura meravigliosa, che mi ricorda quegli archi per le piante rampicanti, si crea tra tRna e mRna, 🧟perché se l'mRna non si lega al DNA per trasformarci in zombie, allora "con chi se la fa"? 👷L'essenza della sintesi proteica (e nel caso del vaccino della fabbricazione della proteina Spike) sta tutta qui, in questa "conversione d'informazioni", che simbolicamente è anche il cuore della divulgazione scientifica. 🐝Le lettere A/P/E rappresentano diversi siti del Ribosoma, che è un po' la discoteca in cui mRna e tRna s'incontrano. 😎A sta per amminoacido (scorrendo si capirà meglio, ma è la fase di "rimorchio" quella in cui tRna "aggancia" mRNA ) 💃🏻P per Papeete, ah no, per Polipeptide (il nome altisonante che la proteina si dà, quando vuole fare la tipa chic e se la tira e s'allunga, con più amminoacidi che cm di tacco ) 👋E per Exit, quando i tRna "scaricano" la proteina e questa se ne esce (incazzata) dal locale (il Ribosoma). La spiegazione è molto metaforica, ma dovrebbe rendere l'idea. 🤞 Condividetelo con chi non prende tutto alla lettera, altrimenti avremo di nuovo problemi con Wuhan 😜 #medicina #medstudents #biologia #biostudent #mrna #trna #sintesiproteica #proteine #divulgazionescientifica #medicinaechirurgia #biology #biologo #genetica #traduzione #ribosomes #amminoacidi #studio #studiare #università #medschool #curiosità #dottori #infermieri #infermieristica #informazione #corpoumano #proteina #protein #chimica #biochimica
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#dottori #biology #università #traduzione #medschool
Jan 31, 2021 14:38
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Si racconta che la farinata sia nata in una notte di tempesta su una nave, in cui vari ingredienti si mescolarono per puro caso. È proprio vero che spesso la realtà supera la fantasia perché il caso supera ogni immaginazione. ~Farinata con yogurt greco~ Farina di ceci, olio, acqua, yogurt greco, sale e rosmarino. #farinatadiceci #healthy #buonappetito #sunday #fit #ceci #protein #lunch #domenica #pranzo #cucinaitaliana #apulia #ifpgallery #yummy #foodphotography #foodie #picoftheday #sharefood #recipes #farinata #foodlover #cucinasana #cookingrecipesrepost #igersitalia #igers #lievitastorie
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#farinatadiceci #lunch #cucinaitaliana #foodie #apulia