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Difference in the energies of interactions at the binding sites in protein structures

โœ Scribed by Pinak Chakrabarti; Sourav Pal

Publisher
Elsevier Science
Year
1993
Tongue
English
Weight
217 KB
Volume
201
Category
Article
ISSN
0009-2614

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โœฆ Synopsis

Biomolecular associations are governed by energetics that influence the stable or the transient nature of various bindings. Ab initio MO calculations on model systems representing a metal ion-carboxylate-water triad in proteins have been performed. Depending on the structural or catalytic role of the water molecule the geometry of interaction and consequently the energy of the ternary systems are found to be different.

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