Journal article
Efforts toward Developing Probes of Protein Dynamics: Vibrational Dephasing and Relaxation of Carbon–Deuterium Stretching Modes in Deuterated Leucine
The journal of physical chemistry. B, Vol.113(23), pp.7991-7994
06/11/2009
DOI: 10.1021/jp900516c
PMID: 19441845
Abstract
The spectral position of C−D stretching absorptions in the so-called “transparent window” of protein absorption (1800−2300 cm−1) makes them well suited as probes of protein dynamics with high temporal and structural resolution. We have previously incorporated single deuterated amino acids into proteins to site-selectively follow protein folding and ligand binding by steady-state FT IR spectroscopy. Ultimately, our goal is to use C−D bonds as probes in time-resolved IR spectroscopy to study dynamics and intramolecular vibrational energy redistribution (IVR) in proteins. As a step toward this goal, we now present the first time-resolved experiments characterizing the population and dephasing dynamics of selectively excited C−D bonds in a deuterated amino acid. Three differently deuterated, Boc-protected leucines were selected to systematically alter the number of additional C−D bonds that may mediate IVR out of the initially populated bright C−D stretching mode. Three-pulse photon echo experiments show that the steady-state C−D absorption linewidths are broadened by both homogeneous and inhomogeneous effects, and transient grating experiments reveal that IVR occurs on a subpicosecond time scale and is nonstatistical. The results have important implications for the interpretation of steady-state C−D spectra and demonstrate the potential utility of C−D bonds as probes of dynamics and IVR within a protein.
Details
- Title: Subtitle
- Efforts toward Developing Probes of Protein Dynamics: Vibrational Dephasing and Relaxation of Carbon–Deuterium Stretching Modes in Deuterated Leucine
- Creators
- Jörg Zimmermann - Department of Chemistry, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla California 92037, and Department of Chemistry, University of Iowa, Iowa City, Iowa 52242Kenan Gundogdu - Department of Chemistry, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla California 92037, and Department of Chemistry, University of Iowa, Iowa City, Iowa 52242Matthew E Cremeens - Department of Chemistry, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla California 92037, and Department of Chemistry, University of Iowa, Iowa City, Iowa 52242Jigar N Bandaria - Department of Chemistry, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla California 92037, and Department of Chemistry, University of Iowa, Iowa City, Iowa 52242Gil Tae Hwang - Department of Chemistry, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla California 92037, and Department of Chemistry, University of Iowa, Iowa City, Iowa 52242Megan C Thielges - Department of Chemistry, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla California 92037, and Department of Chemistry, University of Iowa, Iowa City, Iowa 52242Christopher M Cheatum - Department of Chemistry, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla California 92037, and Department of Chemistry, University of Iowa, Iowa City, Iowa 52242Floyd E Romesberg - Department of Chemistry, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla California 92037, and Department of Chemistry, University of Iowa, Iowa City, Iowa 52242
- Resource Type
- Journal article
- Publication Details
- The journal of physical chemistry. B, Vol.113(23), pp.7991-7994
- DOI
- 10.1021/jp900516c
- PMID
- 19441845
- NLM abbreviation
- J Phys Chem B
- ISSN
- 1520-6106
- eISSN
- 1520-5207
- Publisher
- American Chemical Society
- Language
- English
- Date published
- 06/11/2009
- Academic Unit
- Liberal Arts and Science Admin; Chemistry
- Record Identifier
- 9984217458002771
Metrics
3 Record Views