Article
Solvation Dynamics in Protein Environments: Comparison of Fluorescence Upconversion Measurements of Coumarin 153 in Monomeric Hemeproteins with Molecular Dynamics Simulations
Journal of Chemical Physics
Document Type
Article
Disciplines
Publication Version
Published Version
Publication Date
1-1-2007
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.
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
Copyright Date
2007
Language
en
File Format
application/pdf
Citation Information
Mintu Halder, Prasun Mukherjee, Sayantan Bose, Mark S. Hargrove, et al.. "Solvation Dynamics in Protein Environments: Comparison of Fluorescence Upconversion Measurements of Coumarin 153 in Monomeric Hemeproteins with Molecular Dynamics Simulations" Journal of Chemical Physics Vol. 127 (2007) p. 1 - 6 Available at: http://works.bepress.com/xueyu-song/42/
The following article appeared in Journal of Chemical Physics 127 (2007): 055101, and may be found at doi:10.1063/1.2753495.