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.Full text not available from this repository. (Request a copy)
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|
|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|
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