Fast Dynamics of Halophilic Malate Dehydrogenase and BSA Measured by Neutron Scattering under Various Solvent Conditions Influencing Protein Stability

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 r...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2001-12, Vol.98 (25), p.14356-14361
Hauptverfasser:	Tehei, Moeava, Madern, Dominique, Pfister, Claude, Zaccai, Giuseppe
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Biological Sciences Biology Cattle Circular Dichroism Dehydrogenases Deuterium Oxide Ellipticity Enzyme Stability Haloarcula marismortui Haloarcula marismortui - enzymology In Vitro Techniques Kinetics Malate Dehydrogenase - chemistry Neutron scattering Neutrons Potassium Chloride Protein Folding Protein Structure, Secondary Proteins Salts Scattering, Radiation Serum Albumin, Bovine - chemistry Sodium Chloride Solvents Studies Teeth Thermal stability Thermodynamics Water Wavelengths
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