Integrating Structural Biology and Proteomics for Enhanced Structural Insights.

Abstract

Hydrogen deuterium exchange-MS and Footprinting-MS techniques are capable of predicting the binding site of a binding partner mapped on the protein’s structure deposited in the protein data bank (PDB). Despite these predictions, it frequent discrepancies in the structure information obtained between these MS techniques and PDB data. In this study, we evaluated the structure information derived from MS with 27 high-resolution X-ray crystal structures of human serum albumin to discuss what might be responsible for the discrepancy and to clarify the possibility that structural information obtained by MS can be used to analyze ensemble states in solution. Our findings suggested that MS may become a useful tool for elucidating the structural states of protein conformations in solution under physiological conditions.