Protein folding as a jamming transition.
ArXiv
; 2024 May 15.
Article
em En
| MEDLINE
| ID: mdl-38800654
ABSTRACT
Proteins fold to a specific functional conformation with a densely packed hydrophobic core that controls their stability. We develop a geometric, yet all-atom model for proteins that explains the universal core packing fraction of Ïc=0.55 found in experimental measurements. We show that as the hydrophobic interactions increase relative to the temperature, a novel jamming transition occurs when the core packing fraction exceeds Ïc. The model also recapitulates the global structure of proteins since it can accurately refold to native-like structures from partially unfolded states.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Idioma:
En
Revista:
ArXiv
Ano de publicação:
2024
Tipo de documento:
Article
País de afiliação:
Estados Unidos