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Title:Protein Dynamics And Conformational Heterogeneity Characterized With Two-dimensional Infrared Spectroscopy
Author(s):Thielges, Megan
Contributor(s):Spearman, James; Basom, Edward
Subject(s):Mini-symposium: Spectroscopy in Kinetics and Dynamics
Abstract:Conformational heterogeneity and dynamics impact protein function, but their investigation is limited by the availability of methods for characterizing rapidly fluctuating protein states with both high spatial and temporal resolution. Multidimensional infrared spectroscopy is emerging as a powerful technique that directly probes the structural dynamics on fast timescales. To overcome the spectral congestion inherent to protein spectra that restricts application of infrared spectroscopy to protein systems, we incorporate into proteins vibrational probes with spectrally isolated frequencies and local-mode character that make possible rigorous analysis of protein environments and dynamics with infrared spectroscopy. In particular, both heme-bound carbon monoxide and nitriles selectively incorporated as unnatural amino acids are used as probes of cytochrome P450. 2D IR spectroscopy is used to investigate the impact of protein dynamics and conformational heterogeneity on the selectivity of its catalytic activity. Comparative studies of mutants of cytochrome P450 are used to unravel the contribution of specific residues to the protein's dynamics.
Issue Date:2014-06-17
Publisher:International Symposium on Molecular Spectroscopy
Citation Info:Thielges, M.; Spearman, J.; Basom, E. PROTEIN DYNAMICS AND CONFORMATIONAL HETEROGENEITY CHARACTERIZED WITH TWO-DIMENSIONAL INFRARED SPECTROSCOPY. Proceedings of the International Symposium on Molecular Spectroscopy, Urbana, IL, June 16-21, 2014. DOI: 10.15278/isms.2014.TH13
Genre:Conference Paper / Presentation
Rights Information:Copyright 2014 by the authors. Licensed under a Creative Commons Attribution 4.0 International License.
Date Available in IDEALS:2014-09-17

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