Enzyme-ligand complex; alpha-chymotrypsine; ab initio calculations
Abstract :
[en] Six complexes between a model active site of alpha-chymotrypsin (261 atoms) and N-acetyl-L-tryptophanamide (33 atoms) were optimized at the semiempirical AM1 level. In one of these complexes, a water molecule was included. A detailed study at the geometric and energetic levels is presented. The discussion deals with the nature of the interaction, the effect of the environment, the ligand deformation, the backbone relaxation, the water molecule freedom, and the comparison with the molecular mechanics results.
Research center :
CIP - Centre d'Ingénierie des Protéines - ULiège
Disciplines :
Chemistry
Author, co-author :
Dive, Georges ; Université de Liège - ULiège > Centre d'ingénierie des protéines
Dehareng, Dominique ; Université de Liège - ULiège > Centre d'ingénierie des protéines
Detailed Study of a Molecule in a Molecule N-Acetyl-L-Tryptophanamide in a Active-Site Model of Alpha-Chymotrypsin
Publication date :
1994
Journal title :
Journal of the American Chemical Society
ISSN :
0002-7863
eISSN :
1520-5126
Publisher :
American Chemical Society, Washington, United States - District of Columbia
Volume :
116
Issue :
6
Pages :
2548-2556
Peer reviewed :
Peer Reviewed verified by ORBi
Funders :
BELSPO - SPP Politique scientifique - Service Public Fédéral de Programmation Politique scientifique F.R.S.-FNRS - Fonds de la Recherche Scientifique [BE] FRSM - Fonds de la Recherche Scientifique Médicale [BE] DGTRE - Région wallonne. Direction générale des Technologies, de la Recherche et de l'Énergie [BE]