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Interplay between Secondary and Tertiary Structure Formation in Protein Folding Cooperativity
[Image: see text] Protein folding cooperativity is defined by the nature of the finite-size thermodynamic transition exhibited upon folding: two-state transitions show a free-energy barrier between the folded and unfolded ensembles, while downhill folding is barrierless. A microcanonical analysis, w...
| Autores principales: | , , |
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| Formato: | Texto |
| Lenguaje: | English |
| Publicado: |
American Chemical Society
2010
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| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2944381/ https://www.ncbi.nlm.nih.gov/pubmed/20822175 http://dx.doi.org/10.1021/ja105206w |