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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Veröffentlicht in:	Proc Natl Acad Sci U S A
Hauptverfasser:	Connelly, P R, Thomson, J A
Format:	Artigo
Sprache:	Inglês
Veröffentlicht:	National Academy of Sciences 1992
Schlagworte:	Research Article
Online-Zugang:	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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