The water R1(ω) NMRD profiles of a hydrated protein from molecular dynamics simulation

The hydration of a protein, Peroxiredoxin 5, is obtained from a molecular dynamics simulation and compared with the picture of hydration which is obtained by analysing the water proton R1 NMRD profiles using a generally accepted relaxation model [K. Venu, V. P. Denisov and B. Halle, J. Am. Chem. Soc...

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Bibliographic Details
Published in:Physical chemistry chemical physics : PCCP 2013-01, Vol.15 (33), p.14089-14097
Main Authors: YANG HUANG, KWANGHO NAM, WESTLUND, Per-Olof
Format: Article
Language:English
Subjects:
Biological and medical sciences
Chemistry
Exact sciences and technology
Fundamental and applied biological sciences. Psychology
General and physical chemistry
Molecular biophysics
Molecular Dynamics Simulation
Peroxiredoxins - chemistry
Peroxiredoxins - metabolism
Protein Structure, Tertiary
Protons
Water - chemistry
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Summary:The hydration of a protein, Peroxiredoxin 5, is obtained from a molecular dynamics simulation and compared with the picture of hydration which is obtained by analysing the water proton R1 NMRD profiles using a generally accepted relaxation model [K. Venu, V. P. Denisov and B. Halle, J. Am. Chem. Soc., 1997, 119, 3122]. The discrepancy between the hydration pictures derived from the water R1(ω0)-NMRD profiles and MD is relevant in a discussion of the factors behind the stretched NMRD profile, the distribution of orientational order parameters and residence times of buried water used in the NMRD model.
ISSN:1463-9076
1463-9084
DOI:10.1039/c3cp51147b