Chakrabarti, Pinak ; Pal, Sourav (1993) Difference in the energies of interactions at the binding sites in protein structures Chemical Physics Letters, 201 (1-4). pp. 24-26. ISSN 00092614
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Official URL: http://doi.org/10.1016/0009-2614(93)85027-L
Related URL: http://dx.doi.org/10.1016/0009-2614(93)85027-L
Abstract
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.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to Elsevier B.V |
| ID Code: | 129110 |
| Deposited On: | 08 Nov 2022 10:05 |
| Last Modified: | 08 Nov 2022 10:05 |
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