title: Efforts toward developing direct probes of protein dynamics.
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.
authors: Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.
authors: Matthew E
authors: ME
authors: Cremeens
authors: Hiroshi
authors: H
authors: Fujisaki
authors: Yong
authors: Y
authors: Zhang
authors: Jörg
authors: J
authors: Zimmermann
authors: Laura B
authors: LB
authors: Sagle
authors: Shigeo
authors: S
authors: Matsuda
authors: Philip E
authors: PE
authors: Dawson
authors: John E
authors: JE
authors: Straub
authors: Floyd E
authors: FE
authors: Romesberg