Fast dynamics of halophilic malate dehydrogenase and BSA measured by neutron scattering under various solvent conditions influencing protein stability-Reference-Cited by-同舟云学术

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

Published:2001-12-04 Issue:25 Volume:98 Page:14356-14361
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Tehei M.,Madern D.,Pfister C.,Zaccai G.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference31 articles.

1. Structural Equilibrium Fluctuations in Mesophilic and Thermophilic α-Amylase

2. Unfolded conformations of α-lytic protease are more stable than its native state

3. How Soft Is a Protein? A Protein Dynamics Force Constant Measured by Neutron Scattering

4. A view of dynamics changes in the molten globule-native folding step by quasielastic neutron scattering 1 1Edited by P. E. Wright

5. Protein dynamics: comparison of simulations with inelastic neutron scattering experiments

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