BIOC 212 Lecture Notes - Lecture 2: Phosphatase, Asparagine, Glutamine

• School: McGill University
• Department: Biochemistry
• Course: BIOC 212
• Professor: Arnim Pause

Document Summary

Phosphorylation: phosphorylation on hydroxyl groups, kinases transfer phosphates from atp. January 10th, 2018: specific for side chain and the surrounding peptide sequence, phosphatases remove phosphate also going to be sequence specific, major regulatory mechanism. Phosphopeptide binding: specialized domains bind p-ser, p-thr, or p-tyr, phosphorylation is required for binding, surrounding polypeptide sequence also contributes. Methylation: acetylation of lys amine changes polarity (isopeptide bond) an isopeptide bond is an amide bond that is not present on the main chain of a protein. The bond forms between the carboxyl terminus of one protein and the amino group of a lysine residue on another (target) protein: methylation of lys and arg adds size. Modification binding: like phosphorylation, acetylation and methylation provides new binding sites for proteins, specific domains bind ac-lys, me-lys, me-arg and surrounding sequences. January 10th, 2018: allelic variations, sometimes causing genetic disease.