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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...
Bewaard in:
| Hoofdauteurs: | , |
|---|---|
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
1992
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC49171/ https://ncbi.nlm.nih.gov/pubmed/1375751 |
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