External Force Field for Protein Folding in Chaperonins─Potential Application in <i>In Silico</i> Protein Folding
Irena Roterman, Katarzyna Stąpor, Dawid Dułak, Leszek Konieczny
Abstract
High Resolution Image Download MS PowerPoint Slide 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.