Quantum mechanical map for protein-ligand binding with application to β-trypsin/benzamidine complex

Da W. Zhang, Yun Xiang, Ai M. Gao, John Zhang

Research output: Contribution to journalArticle

Abstract

The benchmark ab initio computation of interaction energies for β-trypsin/benzamidine binding at Hartree-Fock level was reported. Thus, the full ab initio computation was made possible by applying a recently developed molecular fractionation with conjugate caps (MFCC) method. The MFCC method was linear scaling, computationally efficient, and particularly suitable for calculating interaction energy of biopolymers on multiprocessor computer systems.

Original languageEnglish (US)
Pages (from-to)1145-1148
Number of pages4
JournalJournal of Chemical Physics
Volume120
Issue number3
DOIs
StatePublished - Jan 15 2004

Fingerprint

trypsin
caps
fractionation
Trypsin
Fractionation
Ligands
proteins
ligands
biopolymers
Proteins
Biopolymers
interactions
scaling
energy
Computer systems
benzamidine

ASJC Scopus subject areas

  • Atomic and Molecular Physics, and Optics

Cite this

Quantum mechanical map for protein-ligand binding with application to β-trypsin/benzamidine complex. / Zhang, Da W.; Xiang, Yun; Gao, Ai M.; Zhang, John.

In: Journal of Chemical Physics, Vol. 120, No. 3, 15.01.2004, p. 1145-1148.

Research output: Contribution to journalArticle

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