A Hooke's law-based approach to protein folding rate

Kinetics is a key aspect of the renowned protein folding problem. Here, we propose a comprehensive approach to folding kinetics where a polypeptide chain is assumed to behave as an elastic material described by the Hooke[U+05F3]s law. A novel parameter called elastic-folding constant results from our model and is suggested to distinguish between protein with two-state and multi-state folding pathways. A contact-free descriptor, named folding degree, is introduced as a suitable structural feature to study protein-folding kinetics. This approach generalizes the observed correlations between varieties of structural descriptors with the folding rate constant. Additionally several comparisons among structural classes and folding mechanisms were carried out showing the good performance of our model with proteins of different types. The present model constitutes a simple rationale for the structural and energetic factors involved in protein folding kinetics. © 2014 Elsevier Ltd.

• Fecha de publicación: 2015
• Institución: Universidad Tecnológica de Bolívar
• Repositorio: Repositorio Institucional UTB
• Idioma: eng
• OAI Identifier: oai:repositorio.utb.edu.co:20.500.12585/9020
• Acceso en línea: https://hdl.handle.net/20.500.12585/9020
• Palabra clave: Elastic folding constant; Folding degree; Folding kinetics; PROTDCAL; Polypeptide; DNA; Protein; Energetics; Modeling; Peptide; Protein; Reaction kinetics; Amino acid sequence; Article; Elasticity; Protein folding; Protein structure; Structure analysis; Theoretical model; Chemical model; Chemistry; Computer simulation; Kinetics; Protein secondary structure; Thermodynamics; Computer simulation; DNA; Kinetics; Models, Chemical; Protein folding; Protein Structure, Secondary; Proteins; Thermodynamics
• Rights: restrictedAccess
• License: http://creativecommons.org/licenses/by-nc-nd/4.0/