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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...
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| Hlavní autoři: | , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Chemical Society
2010
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| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2944381/ https://ncbi.nlm.nih.gov/pubmed/20822175 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/ja105206w |
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