NDLI: Fast dynamics of halophilic malate dehydrogenase and BSA measured by neutron scattering under various solvent conditions influencing protein stability

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Fast dynamics of halophilic malate dehydrogenase and BSA measured by neutron scattering under various solvent conditions influencing protein stability

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Fast dynamics of halophilic malate dehydrogenase and BSA measured by neutron scattering under various solvent conditions influencing protein stability

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Tehei, M. Pfister, C. Madern, D. Zaccai, G.
Description	Author Affiliation: Tehei M ( Institut de Biologie Structurale, Commissariat à l'Energie Atomique-Centre National de la Recherche Scientifique, 41 rue Jules Horowitz, F-38027 Grenoble Cedex 1, France.);
Abstract	Protein thermal dynamics was evaluated by neutron scattering for halophilic malate dehydrogenase from Haloarcula marismortui (HmMalDH) and BSA under different solvent conditions. As a measure of thermal stability in each case, loss of secondary structure temperatures were determined by CD. HmMalDH requires molar salt and has different stability behavior in H(2)O, D(2)O, and in NaCl and KCl solvents. BSA remains soluble in molar NaCl. The neutron experiments provided values of mean-squared atomic fluctuations at the 0.1 ns time scale. Effective force constants, characterizing the mean resilience of the protein structure, were calculated from the variation of the mean-squared fluctuation with temperature. For HmMalDH, resilience increased progressively with increasing stability, from molar NaCl in H(2)O, via molar KCl in D(2)O, to molar NaCl in D(2)O. Surprisingly, however, the opposite was observed for BSA; its resilience is higher in H(2)O where it is less stable than in D(2)O. These results confirmed the complexity of dynamics-stability relationships in different proteins. Softer dynamics for BSA in D(2)O showed that the higher thermostability is associated with entropic fluctuations. In the halophilic protein, higher stability is associated with increased resilience showing the dominance of enthalpic terms arising from bonded interactions. From previous data, it is suggested that these are associated with hydrated ion binding stabilizing the protein in the high-salt solvent.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	25
Volume Number	98
Language	English
Publisher	National Academy of Sciences
Publisher Date	2001-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Malate Dehydrogenase Chemistry Serum Albumin, Bovine Animals Circular Dichroism Deuterium Oxide Enzyme Stability Haloarcula Marismortui Enzymology In Vitro Techniques Neutrons Potassium Chloride Protein Folding Protein Structure, Secondary Scattering, Radiation Sodium Chloride Solvents Thermodynamics Comparative Study Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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