Campus Units

Biochemistry, Biophysics and Molecular Biology, Chemistry

Document Type

Article

Publication Version

Published Version

Publication Date

2007

Journal or Book Title

Journal of Chemical Physics

Volume

127

First Page

1

Last Page

6

DOI

10.1063/1.2753495

Abstract

The complexes of the fluorescence probe coumarin 153 with apomyoglobin and apoleghemoglobin are used as model systems to study solvation dynamics in proteins.Time-resolved Stokes shift experiments are compared with molecular dynamics simulations, and very good agreement is obtained. The solvation of the coumarin probe is very rapid with approximately 60% occurring within 300fs and is attributed to interactions with water (or possibly to the protein itself). Differences in the solvation relaxation (or correlation) function C(t) for the two proteins are attributed to differences in their hemepockets.

Comments

The following article appeared in Journal of Chemical Physics 127 (2007): 055101, and may be found at doi:10.1063/1.2753495.

Rights

Copyright 2007 American Institute of Physics. This article may be downloaded for personal use only. Any other use requires prior permission of the author and the American Institute of Physics.

Copyright Owner

American Institute of Physics

Language

en

File Format

application/pdf

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