Lysiinijäännöksissä

Lysiinijäännöksissä, often translated as lysine residues, refers to the presence of the amino acid lysine within a protein or peptide structure. Lysine is a basic amino acid, meaning it carries a positive charge at physiological pH due to its side chain's epsilon-amino group. This charge plays a significant role in the overall properties and function of the protein.

The presence of lysine residues is crucial for various biological processes. Their positive charge can mediate electrostatic interactions with negatively charged molecules, such as DNA, RNA, or other proteins. This interaction is vital for DNA packaging in histones, where lysine residues help neutralize the negative phosphate backbone of DNA. Lysine can also be involved in hydrogen bonding and can act as a nucleophile in enzymatic reactions.

Furthermore, lysine residues are common sites for post-translational modifications. One of the most well-known modifications is ubiquitination, where ubiquitin is attached to a lysine residue, marking the protein for degradation or altering its function. Acetylation, methylation, and sumoylation are other important modifications that can occur on lysine side chains, influencing protein stability, localization, and interactions. The specific location and number of lysine residues modified can dictate the outcome of these regulatory events.