Graduate Student Samantha Davila will Present “Analysis of Protein Conformation and Dynamics by Hydrogen/Deuterium Exchange Mass Spectrometry” to the Department
The relationships between structure, function, and dynamics are essential to fully understand a protein. There is no single analytical method capable of providing the extent and range of information required for complete protein analysis. The hydrogen/deuterium (H/D) exchange monitored by mass spectrometry has become a powerful tool for probing conformational dynamics and protein interactions. Deuteriums exchange at the amide hydrogens along the protein’s backbone providing a probe site at each amino acid throughout. Mass spectrometry can effectively monitor the exchange events as mass shifts as a result of the incorporation of deuterium into the protein. The rates of exchange are capable of revealing valuable insight into structural mobility, hydrogen bonding strength, as well as solvent accessibility. Combining proteolysis with the deuterium labeling experiment, under conditions that preserve the exchanges, allows for localizing exchange incidents to specific regions of the protein backbone. H/D exchange mass spectrometry has become a valuable technique for studying conformational dynamics as well as interactions in proteins, protein–ligand and protein–protein complexes.
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