Normal Mode Study of the Internal Dynamics of Various Classes of Cytochrome P450 Enzymes

Abstract

The purpose of this study was to investigate the Cytochrome P450(CYP) enzymes. They constitute a diverse superfamily of more than 8,700 proteins which share a common tertiary fold and only 20% sequence homology. These enzymes are monooxygenases involved in bioactivation, detoxification mechanisms, drug metabolism, and synthesis of normal cellular compounds. In the present study, the Swiss modeling tools ANOLEA and PROCHECK were used to analyze the structures of proteins from each of the six classes of CYP systems. Normal mode analysis through WebNMA was then used to obtain dynamic information. Herein, we will present the preliminary results of our attempt to classify the CYP proteins based on their instrinsic mobility patterns. (CHEM 406 students, Fall 2013)