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This article is about a class of molecules. For protein standard amino acids; however, in certain organisms the
as a nutrient, see Protein (nutrient). For other uses, see genetic code can include selenocysteine andin certain
Protein (disambiguation). archaeapyrrolysine. Shortly after or even during syn-
thesis, the residues in a protein are often chemically mod-
ied by post-translational modication, which alters the
physical and chemical properties, folding, stability, ac-
tivity, and ultimately, the function of the proteins. Some-
times 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 of
time and are then degraded and recycled by the cells ma-
chinery through the process of protein turnover. A pro-
teins 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 12 days in mammalian cells.
Abnormal and 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 es-
sential parts of organisms and participate in virtually
A representation of the 3D structure of the protein myoglobin
every process within cells. Many proteins are enzymes
showing turquoise -helices. This protein was the rst to have
its structure solved by X-ray crystallography. Towards the right-
that catalyse biochemical reactions and are vital to
center among the coils, a prosthetic group called a heme group metabolism. Proteins also have structural or mechanical
(shown in gray) with a bound oxygen molecule (red). functions, such as actin and myosin in muscle and the
proteins in the cytoskeleton, which form a system of
Proteins (/protinz/ or /proti.nz/) are large scaolding that maintains cell shape. Other proteins
biomolecules, or macromolecules, consisting of one are important in cell signaling, immune responses, cell
or more long chains of amino acid residues. Proteins adhesion, and the cell cycle. In animals, proteins are
perform a vast array of functions within organisms, in- needed in the diet to provide the essential amino acids
cluding catalysing metabolic reactions, DNA replication, that cannot be synthesized. Digestion breaks the proteins
responding to stimuli, and transporting molecules from down for use in the metabolism.
one location to another. Proteins dier from one another Proteins may be puried from other cellular components
primarily in their sequence of amino acids, which is using a variety of techniques such as ultracentrifugation,
dictated by the nucleotide sequence of their genes, and precipitation, electrophoresis, and chromatography; the
which usually results in protein folding into a specic advent of genetic engineering has made possible a num-
three-dimensional structure that determines its activity. ber of methods to facilitate purication. Methods com-
A linear chain of amino acid residues is called a monly used to study protein structure and function in-
polypeptide. A protein contains at least one long polypep- clude immunohistochemistry, site-directed mutagenesis,
tide. Short polypeptides, containing less than 2030 X-ray crystallography, nuclear magnetic resonance and
residues, are rarely considered to be proteins and are com- mass spectrometry.
monly 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 dened
by the sequence of a gene, which is encoded in the
genetic code. In general, the genetic code species 20
1
2 2 SYNTHESIS
have attempted to remedy these deciencies by system- molecule substrates. When proteins bind specically to
atically solving representative structures of major fold other copies of the same molecule, they can oligomerize
classes. Protein structure prediction methods attempt to to form brils; this process occurs often in structural pro-
provide a means of generating a plausible structure for teins that consist of globular monomers that self-associate
proteins whose structures have not been experimentally to form rigid bers. Proteinprotein interactions also reg-
determined.[26] ulate enzymatic activity, control progression through the
cell cycle, and allow the assembly of large protein com-
plexes that carry out many closely related reactions with
4 Cellular functions 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 are the chief actors within the cell, said to be proteins allows the construction of enormously complex
carrying out the duties specied by the information en- signaling networks.[29] As interactions between proteins
coded in genes.[5] With the exception of certain types of are reversible, and depend heavily on the availability of
RNA, most other biological molecules are relatively in- dierent groups of partner proteins to form aggregates
ert elements upon which proteins act. Proteins make up that are capable to carry out discrete sets of function,
half the dry weight of an Escherichia coli cell, whereas study of the interactions between specic proteins is a key
other macromolecules such as DNA and RNA make up to understand important aspects of cellular function, and
only 3% and 20%, respectively.[27] The set of proteins ultimately the properties that distinguish particular cell
expressed in a particular cell or cell type is known as its types.[30][31]
proteome.
4.1 Enzymes
conjugated to an extremely electro-dense material, usu- modern organisms and the genes they express. The eld
ally gold. This allows for the localization of both ultra- of bioinformatics is now indispensable for the analysis of
structural details as well as the protein of interest.[50] genes and proteins.
Through another genetic engineering application known
as site-directed mutagenesis, researchers can alter the 5.4.1 Structure prediction and simulation
protein sequence and hence its structure, cellular localiza-
tion, and susceptibility to regulation. This technique even
allows the incorporation of unnatural amino acids into
proteins, using modied tRNAs,[51] and may allow the
rational design of new proteins with novel properties.[52]
5.3 Proteomics
covered the folding of small -helical protein domains from egg whites, blood serum albumin, brin, and wheat
such as the villin headpiece[65] and the HIV accessory gluten.
protein.[66] Hybrid methods combining standard molecu- Proteins were rst described by the Dutch chemist
lar dynamics with quantum mechanical mathematics ex- Gerardus Johannes Mulder and named by the Swedish
plored the electronic states of rhodopsins.[67] chemist Jns Jacob Berzelius in 1838.[72][73] Mulder car-
ried out elemental analysis of common proteins and
5.4.2 Protein disorder and unstructure prediction found that nearly all proteins had the same empirical for-
mula, C400 H620 N100 O120 P1 S1 .[74] He came to the erro-
neous conclusion that they might be composed of a sin-
Many proteins (in Eucaryota ~33%) contain large un-
gle type of (very large) molecule. The term protein
structured but biologically functional segments and can
to describe these molecules was proposed by Mulders
be classied as intrinsically disordered proteins.[68] Pre-
associate Berzelius; protein is derived from the Greek
dicting and analysing protein disorder is, therefore, an im-
word (proteios), meaning primary,[75] in the
portant part of protein structure characterisation.[69]
lead, or standing in front,[76] + -in. Mulder went on to
identify the products of protein degradation such as the
amino acid leucine for which he found a (nearly correct)
6 Nutrition molecular weight of 131 Da.[74]
Early nutritional scientists such as the German Carl von
Further information: Protein (nutrient) Voit believed that protein was the most important nutri-
ent for maintaining the structure of the body, because it
Most microorganisms and plants can biosynthesize all was generally believed that esh makes esh.[77] Karl
20 standard amino acids, while animals (including hu- Heinrich Ritthausen extended known protein forms with
mans) must obtain some of the amino acids from the the identication of glutamic acid. At the Connecticut
diet.[27] The amino acids that an organism cannot synthe- Agricultural Experiment Station a detailed review of
size on its own are referred to as essential amino acids. the vegetable proteins was compiled by Thomas Burr
Key enzymes that synthesize certain amino acids are not Osborne. Working with Lafayette Mendel and apply-
present in animals such as aspartokinase, which catal- ing Liebigs law of the minimum in feeding laboratory
yses the rst step in the synthesis of lysine, methionine, rats, the nutritionally essential amino acids were estab-
and threonine from aspartate. If amino acids are present lished. The work was continued and communicated by
in the environment, microorganisms can conserve energy William Cumming Rose. The understanding of pro-
by taking up the amino acids from their surroundings and teins as polypeptides came through the work of Franz
downregulating their biosynthetic pathways. Hofmeister and Hermann Emil Fischer. The central role
of proteins as enzymes in living organisms was not fully
In animals, amino acids are obtained through the con-
appreciated until 1926, when James B. Sumner showed
sumption of foods containing protein. Ingested pro-
that the enzyme urease was in fact a protein.[78]
teins are then broken down into amino acids through
digestion, which typically involves denaturation of the The diculty in purifying proteins in large quantities
protein through exposure to acid and hydrolysis by en- made them very dicult for early protein biochemists to
zymes called proteases. Some ingested amino acids are study. Hence, early studies focused on proteins that could
used for protein biosynthesis, while others are converted be puried in large quantities, e.g., those of blood, egg
to glucose through gluconeogenesis, or fed into the citric white, various toxins, and digestive/metabolic enzymes
acid cycle. This use of protein as a fuel is particularly im- obtained from slaughterhouses. In the 1950s, the Armour
portant under starvation conditions as it allows the bodys Hot Dog Co. puried 1 kg of pure bovine pancreatic
own proteins to be used to support life, particularly those ribonuclease A and made it freely available to scientists;
found in muscle.[70] Amino acids are also an important this gesture helped ribonuclease A become a major target
dietary source of nitrogen. for biochemical study for the following decades.[74]
Linus Pauling is credited with the successful predic-
tion of regular protein secondary structures based on
7 History and etymology hydrogen bonding, an idea rst put forth by William Ast-
bury in 1933.[79] Later work by Walter Kauzmann on
denaturation,[80][81] based partly on previous studies by
Further information: History of molecular biology
Kaj Linderstrm-Lang,[82] contributed an understanding
of protein folding and structure mediated by hydrophobic
Proteins were recognized as a distinct class of biologi- interactions.
cal molecules in the eighteenth century by Antoine Four-
The rst protein to be sequenced was insulin, by
croy and others, distinguished by the molecules ability
Frederick Sanger, in 1949. Sanger correctly determined
to coagulate or occulate under treatments with heat or
[71] the amino acid sequence of insulin, thus conclusively
acid. Noted examples at the time included albumin
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14 11 EXTERNAL LINKS
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