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Picosecond dynamical changes on denaturation of yeast phosphoglycerate kinase revealed by quasielastic neutron scattering
Author(s) -
Receveur Véronique,
Calmettes Patrick,
Smith Jeremy C.,
Desmadril Michel,
Coddens Gerrit,
Durand Dominique
Publication year - 1997
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199707)28:3<380::aid-prot8>3.0.co;2-g
Subject(s) - picosecond , quasielastic neutron scattering , crystallography , denaturation (fissile materials) , chemistry , protein dynamics , diffusion , superposition principle , neutron scattering , scattering , molecular physics , inelastic neutron scattering , protein structure , thermodynamics , physics , optics , biochemistry , nuclear chemistry , laser , quantum mechanics
Quasielastic neutron scattering experiments performed on yeast phosphoglycerate kinase in the native form and denatured in 1.5 M guanidinium chloride reveal a change in the fast (picosecond time scale) diffusive internal dynamics of the protein. The momentum and energy transfer dependences of the scattering for both states are fitted by an analytical model in which, on the experimentally accessible picosecond time scale and angstrom length scale, the dynamics of a fraction of the nonexchangeable hydrogens in the protein is described as a superposition of vibrations with uniform diffusion in a sphere, the rest of the hydrogens undergoing only vibrational motion. The fraction diffusing changes, from ≈60% in the native protein to ≈82% in the denatured protein. The radius of the sphere also changes slightly, from ≈1.8 Å in the native protein to ≈2.2 Å in the denatured protein. Possible implications of these results for the general protein folding problem are discussed. Proteins 28:380–387, 1997 © 1997 Wiley‐Liss, Inc.