Proliinijäännösten

Proliinijäännösten refers to proline residues in a protein chain. Proline is a unique amino acid due to its side chain, which forms a cyclic structure by bonding back to the amino group of the same amino acid. This structural feature gives proline distinct properties within a polypeptide.

When proline is incorporated into a protein, it restricts the rotation of the peptide backbone, creating kinks or turns in the protein's three-dimensional structure. This often occurs at the end of alpha-helices or within beta-sheets, influencing the overall protein conformation and stability. The immobility introduced by proline residues can be critical for protein folding and function, sometimes acting as regulatory points or structural anchors.

In some cases, proline residues can also participate in post-translational modifications, such as hydroxylation, which is essential for the stability of collagen. The presence and location of proliinijäännösten are therefore important determinants of a protein's structural integrity and biological activity. Understanding the role of these residues is fundamental in fields like molecular biology, biochemistry, and drug discovery.