학술논문
Thermal denaturing of mutant lysozyme with both the OPLSAA and the CHARMM force fields
Document Type
Academic Journal
Source
Journal of the American Chemical Society. Oct 18, 2006, Vol. 128 Issue 41, p13388, 8 p.
Subject
Language
English
ISSN
0002-7863
Abstract
Molecular dynamic simulations are carried out for both the wild-type and the mutant hen lysozyme (TRP62GLY) to study the single mutation effect on lysozyme stability and misfolding. Detailed results show that the single mutation TRP62GLY first induces the loss of the native contacts in the [beta]-domain region of the lysozyme protein at high temperatures, and then the unfolding process spreads in the [alpha]-domain region though Helix C.