Heat capacity changes and hydrophobic interactions in the binding of FK506 and rapamycin to the FK506 binding protein.
Differential interactions among nonpolar moieties at protein/ligand interfaces, and of these nonpolar groups with water, collectively termed hydrophobic interactions, are widely believed to make important energetic contributions to the stability of protein/ligand complexes. Quantitative estimates of...
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| 發表在: | Proc Natl Acad Sci U S A |
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| Principais autores: | , |
| 格式: | Artigo |
| 語言: | Inglês |
| 出版: |
National Academy of Sciences
1992
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| 主題: | |
| 在線閱讀: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC49171/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1375751/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.89.11.4781 |
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