Tertiary Structure Influences the Covalent Labeling Based Structural Analysis of Proteins and Protein Therapeutics

摘要

In intact proteins the microenvironment around weak nucleophilic residues can increase the reactivity of these residues towards covalent labeling with DEPC. The ability to reliably label Ser and Thr residues can improve the structural resolution of covalent labeling - MS method in probing structures of proteins and protein therapeutics. Future direction is to understand what chemical environments most enable the reactivity of Ser and Thr residues. Several other proteins, such as ubiquitin, human growth hormone, and rituximab, will be studied to further confirm our hypothesis.