Dynamic Personality of Proteins and Effect of the Molecular Environment.
J Phys Chem Lett
; 15(20): 5543-5548, 2024 May 23.
Article
en En
| MEDLINE
| ID: mdl-38752860
ABSTRACT
Protein dynamics display distinct traits that are linked to their specific biological function. However, the interplay between intrinsic dynamics and the molecular environment on protein stability remains poorly understood. In this study, we investigate, by incoherent neutron scattering, the subnanosecond time scale dynamics of three model proteins the mesophilic lysozyme, the thermophilic thermolysin, and the intrinsically disordered ß-casein. Moreover, we address the influence of water, glycerol, and glucose, which create progressively more viscous matrices around the protein surface. By comparing the protein thermal fluctuations, we find that the internal dynamics of thermolysin are less affected by the environment compared to lysozyme and ß-casein. We ascribe this behavior to the protein dynamic personality, i.e., to the stiffer dynamics of the thermophilic protein that contrasts the influence of the environment. Remarkably, lysozyme and thermolysin in all molecular environments reach a critical common flexibility when approaching the calorimetric melting temperature.
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Termolisina
/
Caseínas
/
Muramidasa
Idioma:
En
Revista:
J Phys Chem Lett
Año:
2024
Tipo del documento:
Article
País de afiliación:
Italia