TY - JOUR
T1 - Extending Crystallographic Information with Semiempirical Quantum Mechanics and Molecular Mechanics
T2 - A Case of Aspartic Proteinases
AU - Goldblum, Amiram
AU - Rayan, Anwar
AU - Fliess, Amit
AU - Glick, Meir
PY - 1993
Y1 - 1993
N2 - The results of crystallographic analysis of a complex between an aspartic proteinase, endothiapepsin, and an inhibitor have been extended through the assignment of protons in the active site, to study various steps in the reaction with a substrate. Mechanistic implications are suggested as a consequence of semiempirical quantum mechanical calculations, indicating that most of the activation energy is required to bring the substrate from an initial binding mode to close distance to a water molecule.
AB - The results of crystallographic analysis of a complex between an aspartic proteinase, endothiapepsin, and an inhibitor have been extended through the assignment of protons in the active site, to study various steps in the reaction with a substrate. Mechanistic implications are suggested as a consequence of semiempirical quantum mechanical calculations, indicating that most of the activation energy is required to bring the substrate from an initial binding mode to close distance to a water molecule.
UR - http://www.scopus.com/inward/record.url?scp=0027572236&partnerID=8YFLogxK
U2 - 10.1021/ci00012a014
DO - 10.1021/ci00012a014
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C2 - 8391019
AN - SCOPUS:0027572236
SN - 0095-2338
VL - 33
SP - 270
EP - 274
JO - Journal of Chemical Information and Computer Sciences
JF - Journal of Chemical Information and Computer Sciences
IS - 2
ER -