Protein Dynamics And Conformational Heterogeneity Characterized With Two-dimensional Infrared Spectroscopy

Thielges, Megan

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https://hdl.handle.net/2142/51173 Copy

Description

Title

Protein Dynamics And Conformational Heterogeneity Characterized With Two-dimensional Infrared Spectroscopy

Author(s)

Thielges, Megan

Contributor(s)

• Spearman, James
• Basom, Edward

Issue Date

2014-06-17

Keyword(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.

Publisher

International Symposium on Molecular Spectroscopy

Type of Resource

text

Language

English

Permalink

http://hdl.handle.net/2142/51173

DOI

https://doi.org/10.15278/isms.2014.TH13

Copyright and License Information

Copyright 2014 by the authors. Licensed under a Creative Commons Attribution 4.0 International License. http://creativecommons.org/licenses/by/4.0/

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