-PROTEIN- - -KINGDOM OF JOGA-

*/ˈproʊˌtiːnz/ or /ˈproʊti.ɪnz/*

-as of [29 SEPTEMBER 2024]–

(aka “polypeptides”)

-[organic compounds] made of ‘amino acids’ arranged in ‘linear chains’ and folded into ‘globular form’-

(“proteins” are large ‘bio-molecules’ (or ‘macro-molecules’) consisting of 1 or more long chains of ‘amino acid residues’)

(‘proteins’ perform a vast array of ‘functions’ within ‘organisms’, including…)

*catalyzing ‘metabolic reactions’*

*DNA replication*

*responding to ‘stimuli’*

*transporting ‘molecules’ from 1 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 3-dimensional 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; however, in certain organisms the genetic code can include selenocysteine and—in certain archaea—pyrrolysine.

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.

Sometimes 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 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’)

___“PROTEIN TYPES”___

“GLUTEN”

“WHEY PROTEIN”

Protein

Essential and non-essential amino acids

Alanine

Arginine

Aspartic acid
(aspartate)

Asparagine

Cysteine

Glutamic acid
(glutamate)

Glutamine
(may just might)
(as i cackle with delight)