Ordering effect of protein surfaces on water dynamics: NMR relaxation study.
Biophys Chem
; 249: 106149, 2019 06.
Article
em En
| MEDLINE
| ID: mdl-30981137
ABSTRACT
Proteins in solution affect the structural and dynamic properties of the bulk water at the protein-water interface, resulting in a contribution to the order of the hydration water. Theoretical and experimental NMR relaxation methods were developed to study the dynamic properties of water molecules in the protein hydration shell. Water non-selective and selective relaxation rates, were shown to be sensitive to contributions from ordered solvent molecules at protein surface. The average rotational correlation time of water molecules in the protein hydration shell was determined for three protein systems of different size ribonuclease A, human serum albumin and fibrinogen. The knowledge of these properties is an important step toward the determination of the size of the water ordering contributions originate in proteins systems.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Ribonuclease Pancreático
/
Fibrinogênio
/
Água
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Ressonância Magnética Nuclear Biomolecular
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Simulação de Dinâmica Molecular
/
Albumina Sérica Humana
Limite:
Humans
Idioma:
En
Revista:
Biophys Chem
Ano de publicação:
2019
Tipo de documento:
Article