Characterization of the transition state of protein unfolding by use of molecular dynamics: chymotrypsin inhibitor 2.
Temperature-induced unfolding of chymotrypsin inhibitor 2 in water was investigated by molecular dynamics simulations. The major transition state of unfolding was identified on the basis of structural and conformational changes in the protein during the unfolding reaction. The native tertiary contac...
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| Publicado no: | Proc Natl Acad Sci U S A |
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| Principais autores: | , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
National Academy of Sciences
1994
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC45034/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7937969/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.91.22.10430 |
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