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Peptides are short chains of amino acids linked by peptide bonds. [ 1 ] [ 2 ] A polypeptide is a longer, continuous, unbranched peptide chain. [ 3 ] Polypeptides that have a molecular mass of 10,000 Da or more are called proteins . [ 4 ]
The amino acids in a polypeptide chain are linked by peptide bonds between amino and carboxyl group. An individual amino acid in a chain is called a residue, and the linked series of carbon, nitrogen, and oxygen atoms are known as the main chain or protein backbone.
Amino acids are polymerised via peptide bonds to form a long backbone, with the different amino acid side chains protruding along it.In biological systems, proteins are produced during translation by a cell's ribosomes.
Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers – specifically polypeptides – formed from sequences of amino acids, which are the monomers of the polymer. A single amino acid monomer may also be called a residue, which indicates a
Peptide bond formation via dehydration reaction. When two amino acids form a dipeptide through a peptide bond, [1] it is a type of condensation reaction. [2] In this kind of condensation, two amino acids approach each other, with the non-side chain (C1) carboxylic acid moiety of one coming near the non-side chain (N2) amino moiety of the other.
The two amino acid residues are linked through a peptide bond. As both the amine and carboxylic acid groups of amino acids can react to form amide bonds, one amino acid molecule can react with another and become joined through an amide linkage. This polymerization of amino acids is what creates proteins.
A β-strand is a stretch of polypeptide chain typically 3 to 10 amino acids long with backbone in an extended conformation. The supramolecular association of β-sheets has been implicated in the formation of the fibrils and protein aggregates observed in amyloidosis, Alzheimer's disease and other proteinopathies.
Since the peptide bonds themselves are polar they are neutralised by hydrogen bonding with each other when in the hydrophobic environment. This gives rise to regions of the polypeptide that form regular 3D structural patterns called secondary structure. There are two main types of secondary structure: α-helices and β-sheets. [citation needed]