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 language | English (US) |
|---|---|
| Pages (from-to) | 1145-1148 |
| Number of pages | 4 |
| Journal | Journal of Chemical Physics |
| Volume | 120 |
| Issue number | 3 |
| DOIs | |
| State | Published - Jan 15 2004 |
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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 journal › Article
}
TY - JOUR
T1 - Quantum mechanical map for protein-ligand binding with application to β-trypsin/benzamidine complex
AU - Zhang, Da W.
AU - Xiang, Yun
AU - Gao, Ai M.
AU - Zhang, John
PY - 2004/1/15
Y1 - 2004/1/15
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=1142279661&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=1142279661&partnerID=8YFLogxK
U2 - 10.1063/1.1639152
DO - 10.1063/1.1639152
M3 - Article
VL - 120
SP - 1145
EP - 1148
JO - Journal of Chemical Physics
JF - Journal of Chemical Physics
SN - 0021-9606
IS - 3
ER -