Structural highlights
Function
THER_BACTH Extracellular zinc metalloprotease.
Publication Abstract from PubMed
The hydrophobic effect is associated with the successive replacement of water molecules in the binding site of a protein by hydrophobic groups of the ligand. Although the hydrophobic effect is assumed to be entropy-driven, large changes in enthalpy and entropy are observed with the model system thermolysin. Structural changes in the binding features of the water molecules ultimately determine the thermodynamics of the hydrophobic effect.
Dissecting the hydrophobic effect on the molecular level: the role of water, enthalpy, and entropy in ligand binding to thermolysin.,Biela A, Nasief NN, Betz M, Heine A, Hangauer D, Klebe G Angew Chem Int Ed Engl. 2013 Feb 4;52(6):1822-8. doi: 10.1002/anie.201208561., Epub 2013 Jan 2. PMID:23283700[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Biela A, Nasief NN, Betz M, Heine A, Hangauer D, Klebe G. Dissecting the hydrophobic effect on the molecular level: the role of water, enthalpy, and entropy in ligand binding to thermolysin. Angew Chem Int Ed Engl. 2013 Feb 4;52(6):1822-8. doi: 10.1002/anie.201208561., Epub 2013 Jan 2. PMID:23283700 doi:http://dx.doi.org/10.1002/anie.201208561
