External Force Field for Protein Folding in Chaperonins-Potential Application in In Silico Protein Folding.

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.

SUBMITTER: Roterman I 

PROVIDER: S-EPMC11044213 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature