Ghosh, I and Rao, VS (1984) Effect of configuration of the inhibitors on the mode of binding to the enzyme, thermolysin. In: Journal of Biomolecular Structure and Dynamics, 22 (1). pp. 29-40.
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Abstract
Preferred conformations of the competitive inhibitors glycyl-L-phenylalanine and glycyl-D-phenylalanine and their mode of binding to thermolysin have been studied. The difference in configuration is shown to affect significantly the mode of binding to thermolysin. Gly-D-Phe prefers to enter the active site in the global minimum conformation whereas Gly-L-Phe may enter in a higher energy conformation. Moreover, D-enantiomer is shown to have a better fit than the L-counterpart in the active site.
| Item Type: | Journal Article |
|---|---|
| Publication: | Journal of Biomolecular Structure and Dynamics |
| Publisher: | Adenine Presses |
| Additional Information: | Copyright of this article belongs to Adenine Presses. |
| Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit |
| Date Deposited: | 10 Aug 2009 09:56 |
| Last Modified: | 10 Aug 2009 09:56 |
| URI: | http://eprints.iisc.ac.in/id/eprint/21987 |
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