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Efforts toward developing direct probes of protein dynamics

Academic Article
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Overview

authors

  • Cremeens, M. E.
  • Fujisaki, H.
  • Zhang, Y.
  • Zimmermann, J.
  • Sagle, L. B.
  • Matsuda, S.
  • Dawson, Philip
  • Straub, J. E.
  • Romesberg, Floyd

publication date

  • May 2006

journal

  • Journal of the American Chemical Society  Journal

abstract

  • We report the first IR characterization of a single C-D bond within a protein, methyl-d1 Met80 of horse heart cytochrome c. A comparison was made to methyl-d1/d3 methionine as well as methyl-d3 Met80. We found that for methyl-d1 and the asymmetric stretches of methyl-d3, line widths/line shapes are dominated by inhomogeneous broadening, whereas the symmetric stretch of methyl-d3 has a significant homogeneous component. Vibrational energy relaxation calculations found that a significantly stronger Fermi resonance exists for the symmetric stretch than for the asymmetric stretches, thereby suggesting that a difference in intramolecular vibrational relaxation (IVR) causes the observed line width/line shape difference between the symmetric and asymmetric stretches.

subject areas

  • Animals
  • Cytochromes c
  • Deuterium
  • Horses
  • Methionine
  • Models, Molecular
  • Protein Conformation
  • Quantum Theory
  • Spectrophotometry, Infrared
  • Thermodynamics
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Identity

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja061328g

PubMed ID

  • 16669659
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Additional Document Info

start page

  • 6028

end page

  • 6029

volume

  • 128

issue

  • 18

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