External Force Field for Protein Folding in Chaperonins-Potential Application in In Silico Protein Folding.
ACS Omega
; 9(16): 18412-18428, 2024 Apr 23.
Article
em En
| MEDLINE
| ID: mdl-38680295
ABSTRACT
The present study discusses the influence of the TRiC chaperonin involved in the folding of the component of reovirus mu1/σ3. The TRiC chaperone is treated as a provider of a specific external force field in the fuzzy oil drop model during the structural formation of a target folded protein. The model also determines the status of the final product, which represents the structure directed by an external force field in the form of a chaperonin. This can be used for in silico folding as the process is environment-dependent. The application of the model enables the quantitative assessment of the folding dependence of an external force field, which appears to have universal application.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Idioma:
En
Revista:
ACS Omega
Ano de publicação:
2024
Tipo de documento:
Article
País de afiliação:
Polônia
País de publicação:
Estados Unidos