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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...

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Autors principals: Connelly, P R, Thomson, J A
Format: Artigo
Idioma:Inglês
Publicat: 1992
Matèries:
Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC49171/
https://ncbi.nlm.nih.gov/pubmed/1375751
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