Title: Insights into enzyme structure and dynamics elucidated by amide H/D exchange mass spectrometry.

Authors: Busenlehner, Laura S; Armstrong, Richard N

Published In Arch Biochem Biophys, (2005 Jan 01)

Abstract: Conformational changes and protein dynamics play an important role in the catalytic efficiency of enzymes. Amide H/D exchange mass spectrometry (H/D exchange MS) is emerging as an efficient technique to study the local and global changes in protein structure and dynamics due to ligand binding, protein activation-inactivation by modification, and protein-protein interactions. By monitoring the selective exchange of hydrogen for deuterium along a peptide backbone, this sensitive technique probes protein motions and structural elements that may be relevant to allostery and function. In this report, several applications of H/D exchange MS are presented which demonstrate the unique capability of amide hydrogen/deuterium exchange mass spectrometry for examining dynamic and structural changes associated with enzyme catalysis.

PubMed ID: 15581564

MeSH Terms: Amides/chemistry*; Binding Sites; Catalysis; Catalytic Domain; Crystallography, X-Ray; Deuterium/chemistry*; Enzymes/chemistry*; Enzymes/metabolism*; Forecasting; Hydrogen/chemistry*; Ligands; Mass Spectrometry/methods*; Models, Chemical; Models, Molecular; Molecular Structure; Peptides/chemistry; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Protein Subunits/chemistry; Protein Subunits/metabolism; Proteins/chemistry; Proteins/metabolism; Sensitivity and Specificity