Title

Thermochemical Differences in Isomeric Oligopeptides: Structural Insights using IRMPD Spectroscopy

Lead Author Affiliation

Bioanalytical & Physical Chemistry/Department of Chemistry

Introduction

For many proteins, unusual shifts in pKa can be observed for certain active site residues- drastically changing its reactivity. Our group is interested in fundamentally studying the origin of these changes in reactivity by studying simple model oligopeptide systems that can emulate a protein’s active site. From our previous studies, we have demonstrated that isomeric oligopeptides containing the same types of residues have clear differences in proton affinities due to subtle differences in their structure. Although structure can be predicted using computational modeling, mass spectrometric methods in conjunction with infrared spectroscopy and computational chemistry enables us to determine gas-phase structure and to explain the origin of these proton affinity differences.

Location

DUC Ballroom A&B

Format

Poster Presentation

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Apr 30th, 1:00 PM Apr 30th, 3:30 PM

Thermochemical Differences in Isomeric Oligopeptides: Structural Insights using IRMPD Spectroscopy

DUC Ballroom A&B

For many proteins, unusual shifts in pKa can be observed for certain active site residues- drastically changing its reactivity. Our group is interested in fundamentally studying the origin of these changes in reactivity by studying simple model oligopeptide systems that can emulate a protein’s active site. From our previous studies, we have demonstrated that isomeric oligopeptides containing the same types of residues have clear differences in proton affinities due to subtle differences in their structure. Although structure can be predicted using computational modeling, mass spectrometric methods in conjunction with infrared spectroscopy and computational chemistry enables us to determine gas-phase structure and to explain the origin of these proton affinity differences.