Cooperativity and protein folding rates
| Autor: | John J. Portman |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
chemistry.chemical_classification
Protein Folding Quantitative Biology::Biomolecules genetic structures Globular protein Proteins Cooperativity Phi value analysis Kinetics Crystallography chemistry Structural Biology Chemical physics Proteins metabolism Thermodynamics Protein folding Downhill folding Molecular Biology |
| Zdroj: | Current Opinion in Structural Biology. 20:11-15 |
| ISSN: | 0959-440X |
| DOI: | 10.1016/j.sbi.2009.12.013 |
| Popis: | Despite the large and complex conformational space available to an unfolded protein, many small globular proteins fold with simple two-state cooperative kinetics. Understanding what determines folding rates beyond simple rules summarizing kinetic trends has proved to be more elusive than predicting folding mechanism. Topology-based models with smooth energy landscapes give reasonable predictions of the structure of the transition state ensemble, but do not have the kinetic or thermodynamic cooperativity exhibited by two-state proteins. This review outlines some recent efforts to understand what determines the cooperativity and the diversity of folding rates of two-state folding proteins. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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