학술논문
Tracking conformational states in allosteric transitions of phosphorylase
Document Type
Academic Journal
Source
Biochemistry. Nov 24, 1992, Vol. 31 Issue 46, p11297, 8 p.
Subject
Language
ISSN
0006-2960
Abstract
A study was conducted to test the effectivity of a method for visualizing protein domain movements. The method calculates the principal axes of a protein domain based on the inertia tensor matrix. The axes in turn are used to create an ellipsoid representing the shape of the protein domain. This method was tested on the domain of phosphorylase. Although the obtained domain movements were found to be characteristic of phosphorylase structures, the activation domain was found to move as a rigid body and therefore its motion was not easily examined.