Ghosh, Indira and Rao, VSR (1982) A conformational approach to the study of the dynamics of enzyme inhibition: studies on thermolysin. In: International Journal of Biological Macromolecules, 4 (3). pp. 130-136.
fulltext.pdf - Published Version
Restricted to Registered users only
Download (665Kb) | Request a copy
The preferred conformations of β-phenylpropionyl-Image -phenylalanine (β-PPP) and N-carbobenzoxy-L-phenylalanine (Cbz-Phe), two inhibitors of thermolysin, have been determined by computing potential energy using empirial potential energy functions. Of the 15 to 20 conformations that are favoured for each of these inhibitors only a few have the right conformation to reach the active site of the enzyme. The conformer of β-PPP that initiates binding with the enzyme is different from the bound one, while for Cbz-Phe the bound and initiating conformers are quite similar. Thus, β-PPP favours the ‘induced fit’ model while Cbz-Phe follows the ‘lock and key’ model of binding. The inhibitors differ in their alignment at the active site.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Elsevier Science.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||04 Aug 2009 02:48|
|Last Modified:||19 Sep 2010 05:39|
Actions (login required)