nutrition title image nutrition information site logo


top url strip


A representation of the 3D structure of myoglobin, showing coloured alpha helices. This protein was the first to have its structure solved by X-ray crystallography by Max Perutz and Sir John Cowdery Kendrew in 1958, which led to them receiving a Nobel Prize in Chemistry.

A protein is a complex, high-molecular-weight organic compound that consists of amino acids joined by peptide bonds. Proteins are essential to the structure and function of all living cells and viruses. Many proteins are enzymes or subunits of enzymes. Other proteins play structural or mechanical roles, such as those that form the struts and joints of the cytoskeleton, serving as biological scaffolds for the mechanical integrity and tissue signalling functions. Still more functions filled by proteins include immune response and the storage and transport of various ligands. In nutrition, proteins serve as the source of amino acids for organisms that do not synthesize those amino acids natively.

Proteins are one of the classes of bio-macromolecules, alongside polysaccharides, lipids, and nucleic acids, that make up the primary constituents of living things. They are among the most actively-studied molecules in biochemistry, and were discovered by Jöns Jakob Berzelius in 1838.

Almost all natural proteins are encoded by DNA. DNA is transcribed to yield RNA, which serves as a template for translation by ribosomes.

Properties of Proteins

Proteins are amino acid chains that fold into unique 3-dimensional structures. The shape into which a protein naturally folds is known as its native state, which is determined by its sequence of amino acids. Biochemists refer to four distinct aspects of a protein's structure:

* Primary structure: the amino acid sequence
* Secondary structure: highly patterned sub-structures—alpha helix and beta sheet—or segments of chain that assume no stable shape. Secondary structures are locally defined, meaning that there can be many different secondary motifs present in one single protein molecule.
* Tertiary structure: the overall shape of a single protein molecule; the spatial relationship of the secondary structural motifs to one another
* Quaternary structure: the shape or structure that results from the union of more than one protein molecule, usually called subunit proteins subunits in this context, which function as part of the larger assembly or protein complex.

In addition to these levels of structure, proteins may shift between several similar structures in performing their biological function. 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.

Proteins are separated into two groups: Complete and Incomplete. Incomplete proteins are from plants and do not include all 20 amino acids. Complete proteins come from an animal and include all 20 amino acids. You get protein from mostly everything you eat, but whether all the amino acids are in them depends on what the substance is.

The primary structure is held together by covalent peptide bonds, which are made during the process of translation. The secondary structures are held together by hydrogen bonds. The tertiary structure is held together primarily by hydrophobic interactions but hydrogen bonds, ionic interactions, and disulfide bonds are usually involved too.

The process by which the higher structures form is called protein folding and is a consequence of the primary structure. The mechanism of protein folding is not entirely understood. Although any unique polypeptide may have more than one stable folded conformation, each conformation has its own biological activity and only one conformation is considered to be the active, or native conformation.

The two ends of the amino acid chain are referred to as the carboxy terminus (C-terminus) and the amino terminus (N-terminus) based on the nature of the free group on each extremity.

Working with proteins

Proteins are sensitive to their environment. They may only be active in their native state, over a small pH range, and under solution conditions with a minimum quantity of electrolytes. A protein in its native state is often described as folded. A protein that is not in its native state is said to be denatured. Denatured proteins generally have no well-defined secondary structure. Many proteins denature and will not remain in solution in distilled water.

One of the more striking discoveries of the 20th century was that the native and denatured states in many proteins were interconvertible, that by careful control of solution conditions (by for example, dialyzing away a denaturing chemical), a denatured protein could be converted to native form. The issue of how proteins arrive at their native state is an important area of biochemical study, called the study of protein folding.

Through genetic engineering, researchers can alter the sequence and hence the structure, "targeting", susceptibility to regulation and other properties of a protein. The genetic sequences of different proteins may be spliced together to create "chimeric" proteins that possess properties of both. This form of tinkering represents one of the chief tools of cell and molecular biologists to change and to probe the workings of cells. Another area of protein research attempts to engineer proteins with entirely new properties or functions, a field known as protein engineering.

Protein-protein interactions can be screened for using two-hybrid screening.

Protein regulation

Various molecules and ions are able to bind to specific sites on proteins. These sites are called binding sites. They exhibit chemical specificity. The particle that binds is called a ligand. The strength of ligand-protein binding is a property of the binding site known as affinity.

Since proteins are involved in practically every function performed by a cell, the mechanisms for controlling these functions therefore depend on controlling protein activity. Regulation can involve a protein's shape or concentration. Some forms of regulation include:

* Allosteric modulation: When the binding of a ligand at one site on a protein affects the binding of ligand at another site.
* Covalent modulation: When the covalent modification of a protein affects the binding of a ligand or some other aspect of the protein's function.


Proteins are generally large molecules, having molecular masses of up to 3,000,000 (the muscle protein titin has a single amino acid chain 27,000 subunits long). Such long chains of amino acids are almost universally referred to as proteins, but shorter strings of amino acids are referred to as "polypeptides," "peptides" or rarely, "oligopeptides". The dividing line is undefined, though "polypeptide" usually refers to an amino acid chain lacking tertiary structure which may be more likely to act as a hormone (like insulin), rather than as an enzyme (which depends on its defined tertiary structure for functionality).

Proteins are generally classified as soluble, filamentous or membrane-associated (see integral membrane protein). Nearly all the biological catalysts known as enzymes are soluble proteins (with a recent notable execption being the discovery of ribozymes, RNA molecules with the catalytic properties of enzymes.) Antibodies, the basis of the adaptive immune system, are another example of soluble proteins. Membrane-associated proteins include exchangers and ion channels, which move their substrates from place to place but do not change them; receptors, which do not modify their substrates but may simply shift shape upon binding them. Filamentous proteins make up the cytoskeleton of cells and much of the structure of animals: examples include tubulin, actin, collagen and keratin, all of which are important components of skin, hair, and cartilage. Another special class of proteins consists of motor proteins such as myosin, kinesin, and dynein. These proteins are "molecular motors," generating physical force which can move organelles, cells, and entire muscles.

Role of Protein


Proteins are involved in practically every function performed by a cell, including regulation of cellular functions such as signal transduction and metabolism. For example, protein catabolism requires enzymes termed proteases and other enzymes such as glycosidases.

Within Nutrition

Protein is an important macronutrient to the human diet, supplying the body's needs for nitrogen and amino acids, the building blocks of proteins. The exact amount of dietary protein needed to satisfy these requirements may vary widely depending on age, sex, level of physical activity, and medical condition, as well as the RDA specified by the state.

The reccomended intake of protein differs from country to country, but it is marginalised between 0.8 and 1.2g / kg b.w (Per kilogram of bodyweight), however , in more serious athletes, requiring strength, the figure is somewhat between 1.0 and 2.0g per kilogram of Body weight, which is referred to as the maximum protein intake:benefits ratio. Although Proteins are found in all foods, be it only in small amounts, protein is still well concentrated in foods such as legumes, nuts, meat, and dairy products the majority of which are protein choices for vegetarians.

Protein is the major component in the regulation, growth and differentation of muscles, tendons, enzymes, skin, hair, eyes, as well as a tremendous variety of other organs and processes. The quality of protein intake is particularly important because different proteins supply essential amino acids in different proportions. Given an adequate intake of nitrogen, the human body can manufacture 10 of the 18 amino acids from glucose. The remaining 8 amino acids (threonine, valine, tryptophan, isoleucine, leucine, lysine, phenylalanine, and methionine) cannot be manufactured by the body and must be acquired through supplementation. Thus, they are termed essential amino acids.

For use within the body, the majority of protein taken from food consumed is converted by protein catabolism into ammonia which, due to its toxicity, must be converted to either urea or uric acid,or in some animals is excreted in urine. Proteins possessing equal proportions of all essential amino acids in relatively abundant quantities are often termed "complete", or "High-Quality" Proteins, which are generally obtained from Animal Proteins, such as meat, and are rated using PDCAAS (Protein Digestibility Corrected Amino Acid Score).

Despite what the name suggests, quality proteins are not essential for good supplementation or nutrition within the average person, however, the difference between Amino Acids in Plant and Animal proteins is discernable, particularly for athletes or bodybuilders as Plant Proteins lack two major Amino acids found in Animal proteins ; Lysine within Grains, and Methionine within Legumes, major benefactors to a major athlete's dietary regime. Neverthelss, in terms of quality, amino acids found in Plant and Animal extracts are identical.

Protein deficiency can lead to symptoms such as fatigue, insulin resistance, hair loss, loss of hair pigment, loss of muscle mass , low body temperature, hormonal irregularities, as well as loss of skin elsaticity. Severe protein deficiency, encountered only in times of famine, is fatal, due to the lack of material for the body to facilitate as energy.

It has been known that in some "wild diets", in which people lose mass amounts of weight in a short period of time are attributed to deficiencies in Protein, and thus loss in muscle mass, and not fat, which is widely known as a dangerous practice, particularly because of the benefits of Muscle mass over Fat.

Excessive protein intake has also been linked to several problems -

* overreaction within the immune system
* liver dysfunction due to increased toxic residues
* loss of bone density, frailty of bones due to increased acidity in the blood and foundering (foot problems) in horses.

It is assumed by reasearchers on the field, that excessive intake of protein forced increased calcium excretion. If there is to be excessive intake of protein, it is thought that a regular intake of calcium would be able to stablilise, or even increase the uptake of calcium by the small intestine, which would be more beneficial in older women.

Proteins are often progenitors in allergies and allergic reactions to certain foods. This is because the structure of each form of protein is slightly different; some may trigger a response from the immune system while others remain perfectly safe. Many people are allergic to casein, the protein in milk; gluten, the protein in wheat and other grains; the particular proteins found in peanuts; or those in shellfish or other seafoods. It is extremely unusual for the same person to adversely react to more than two different types of proteins, due to the diversity between Protein or Amino Acid types.

Go to home page of nutrition | Sources and Attributions

Automatic Backlinks



bottom copyright strip