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Understanding the determinants of stability and folding of small globular proteins from their energetics
The results of minimal model calculations indicate that the stability and the kinetic accessibility of the native state of small globular proteins are controlled by few “hot” sites. By means of molecular dynamics simulations around the native conformation, which describe the protein and the surround...
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| Hlavní autoři: | , , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Cold Spring Harbor Laboratory Press
2004
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| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2286534/ https://ncbi.nlm.nih.gov/pubmed/14691227 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.03223804 |
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