External Force Field for Protein Folding in Chaperonins-Potential Application in Protein Folding

Overview

Journal ACS Omega

Publisher American Chemical Society

Specialty Chemistry

Date 2024 Apr 29

PMID 38680295

Authors

Irena Roterman

Katarzyna Stapor

Dawid Dulak

Leszek Konieczny

Affiliations

Soon will be listed here.

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 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.

Citing Articles

Protein folding: Funnel model revised.

Roterman I, Slupina M, Konieczny L Comput Struct Biotechnol J. 2024; 23:3827-3838.

PMID: 39525086 PMC: 11550765. DOI: 10.1016/j.csbj.2024.10.030.

Domain swapping: a mathematical model for quantitative assessment of structural effects.

Roterman I, Stapor K, Dulak D, Konieczny L FEBS Open Bio. 2024; 14(12):2006-2025.

PMID: 39370305 PMC: 11609593. DOI: 10.1002/2211-5463.13911.

Hydrophobicity-Based Force Field In Enzymes.

Roterman I, Konieczny L, Stapor K, Slupina M ACS Omega. 2024; 9(7):8188-8203.

PMID: 38405467 PMC: 10882594. DOI: 10.1021/acsomega.3c08728.

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