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RESEARCH PRODUCT
A Hooke's law-based approach to protein folding rate
Yovani Marrero-ponceJesus SalgadoYasser B. Ruiz-blancoYamila GarcíaC. M. Sotomayor-torresC. M. Sotomayor-torresPablo J. Prietosubject
Statistics and ProbabilityPROTDCALStructure analysisGeneral Biochemistry Genetics and Molecular BiologyArticleProtein Structure SecondaryAmino acid sequencesymbols.namesakeProtein structureEnergeticsFeature (machine learning)Statistical physicsProtein foldingTheoretical modelProtein secondary structureReaction kineticsGeneral Immunology and MicrobiologyChemical modelApplied MathematicsProteinHooke's lawModelingProteinsGeneral MedicineDNAComputer simulationElasticityFolding degreeFolding (chemistry)ChemistryKineticsModels ChemicalModeling and SimulationPeptidesymbolsProtein structureElastic folding constantPhysical chemistryProtein secondary structureThermodynamicsProtein foldingDownhill foldingPolypeptideGeneral Agricultural and Biological SciencesConstant (mathematics)Folding kineticsdescription
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.
year | journal | country | edition | language |
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2014-06-04 |