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Φ-Value analysis by molecular dynamics simulations of reversible folding

In Φ-value analysis, the effects of mutations on the folding kinetics are compared with the corresponding effects on thermodynamic stability to investigate the structure of the protein-folding transition state (TS). Here, molecular dynamics (MD) simulations (totaling 0.65 ms) have been performed for...

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Pubblicato in:Proc Natl Acad Sci U S A
Autori principali: Settanni, Giovanni, Rao, Francesco, Caflisch, Amedeo
Natura: Artigo
Lingua:Inglês
Pubblicazione: National Academy of Sciences 2005
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Accesso online:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC545520/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/15644439/
https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.0406754102
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