Efforts toward developing direct probes of protein dynamics

被引:48
作者
Cremeens, Matthew E.
Fujisaki, Hiroshi
Zhang, Yong
Zimmermann, Joerg
Sagle, Laura B.
Matsuda, Shigeo
Dawson, Philip E.
Straub, John E.
Romesberg, Floyd E.
机构
[1] Scripps Res Inst, Dept Chem, La Jolla, CA 92037 USA
[2] Boston Univ, Dept Chem, Boston, MA 02215 USA
关键词
D O I
10.1021/ja061328g
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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. Copyright © 2006 American Chemical Society.
引用
收藏
页码:6028 / 6029
页数:2
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