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Time-resolved Stokes shift in proteins with continuum model: Slow dynamics in proteins

Paper ID Volume ID Publish Year Pages File Format Full-Text
27798 44043 2010 8 PDF Available
Title
Time-resolved Stokes shift in proteins with continuum model: Slow dynamics in proteins
Abstract

Reported time-resolved Stokes shifts (TRSS) of free tryptophan (Trp) and free p-coumaric acid (CA) in water, and Trp in monellin, apomyoglobin, and isoalloxazine (Iso) of flavin mononucleotide (FMN) in the reductase component (C1 protein) of p-hydroxyphenylacetate hydroxylase were analyzed with continuum model. All unknown parameters of these systems in the theoretical equations were determined to obtain the best fit between the observed and calculated TRSS, according to a non-linear least square method. TRSS of free Trp at 295 K was also analyzed with four sets of reported dielectric constants and solvent relaxation times of water. Agreement between the observed and calculated TRSS of the free Trp was excellent. In CA the calculated TRSS could satisfactorily reproduce the observed one. Frequency-dependent dielectric constants of Trp in the proteins and Iso in C1 protein were expressed with 2- and 3-relaxation times. Static dielectric constant, ɛ0, intermediate permittivity, ɛ1, dielectric constant of Iso, ɛc, 2-relaxation times, τ1 and τ2, μe and D0 in the 2-relaxation time analyses were determined by the best-fit procedures. Agreements between the observed and calculated TRSS of Trp in native, denatured monellins, apomyoglobin, and Iso in C1 protein were excellent. No further improvements were obtained with 3-relaxation time analyses. Origin of the slow decaying component of TRSS in apomyoglobin was interpreted with continuum model and compared with molecular dynamics (MD) simulation model and a continuum model by Halle and Nilsson [J. Phys. Chem. B 113 (2009) 8210]. Frozen states revealed with MD model were reproduced with the 3-relaxation time analysis.

Keywords
Tryptophan; Protein; Time-resolved Stokes shift; Flavin; C1 protein; Theoretical analyses; Continuum model
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology A: Chemistry - Volume 215, Issue 1, 5 September 2010, Pages 38–45
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us