Glycerol-slaved 1H-1H NMR cross-relaxation in quasi-native lysozyme.
Biophys Chem
; 312: 107286, 2024 Sep.
Article
em En
| MEDLINE
| ID: mdl-38964115
ABSTRACT
1H-1H nuclear cross-relaxation experiments have been carried out with lysozyme in variable glycerol viscosity to study intramolecular motion, self-diffusion, and isotropic rigid-body rotational tumbling at 298 K, pH 3.8. Dynamics of intramolecular 1H-1H cross-relaxation rates, the increase in internuclear spatial distances, and lateral and rotational diffusion coefficients all show fractional viscosity dependence with a power law exponent κ in the 0.17-0.83 range. The diffusion coefficient of glycerol Ds with the bulk viscosity itself is non-Stokesian, having a fractional viscosity dependence on the medium viscosity (Ds ⼠η-κ, κ ≈ 0.71). The concurrence and close similarity of the fractional viscosity dependence of glycerol diffusion on the one hand, and diffusion and intramolecular cross-relaxation rates of the protein on the other lead to infer that relaxation of glycerol slaves protein relaxations. Glycerol-transformed native lysozyme to a quasi-native state does not affect the conclusion that both global and internal fluctuations are slaved to glycerol relaxation.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Muramidase
/
Glicerol
Limite:
Animals
Idioma:
En
Revista:
Biophys Chem
Ano de publicação:
2024
Tipo de documento:
Article