QUANTUM CHEMICAL CALCULATION OF THE ENZYME-LIGAND INTERACTION ENERGY FOR TRYPSIN INHIBITION BY BENZAMIDINES.

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

Three-dimensional coordinates of the beta -trypsin-benzamidine complex were used to construct a quantum chemical model for the enzyme-inhibitor interaction. The model included all enzyme and benzamidinium (H//4N//2CC//6H//4X** plus ) atoms and two bound water molecules (W702 and W710) located near the binding site. Hydration was also treated by using a simple model of the first hydration sphere including four water molecules. The enzyme-inhibitor interaction energy was approximated as SIGMA V//e//n//z(r//a)qa, where the first term is the enzyme electrostatic potential at the position of atom a and the second term is the charge of this atom. The potential was calculated from bond fragments as proposed previously while net charges were obtained from CNDO/2 calculations.

Original languageEnglish
Pages (from-to)4584-4589
Number of pages6
JournalJournal of the American Chemical Society
Volume106
Issue number16
Publication statusPublished - Aug 8 1984

Fingerprint

Benzamidines
Enzyme inhibition
Enzyme Inhibitors
Trypsin
Enzymes
Ligands
Chemical Models
Hydration
Atoms
Water
Static Electricity
Molecules
Binding Sites
Electrostatics
Binding sites

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

@article{5215bc0ffc504abf815853e2149d4e1a,
title = "QUANTUM CHEMICAL CALCULATION OF THE ENZYME-LIGAND INTERACTION ENERGY FOR TRYPSIN INHIBITION BY BENZAMIDINES.",
abstract = "Three-dimensional coordinates of the beta -trypsin-benzamidine complex were used to construct a quantum chemical model for the enzyme-inhibitor interaction. The model included all enzyme and benzamidinium (H//4N//2CC//6H//4X** plus ) atoms and two bound water molecules (W702 and W710) located near the binding site. Hydration was also treated by using a simple model of the first hydration sphere including four water molecules. The enzyme-inhibitor interaction energy was approximated as SIGMA V//e//n//z(r//a)qa, where the first term is the enzyme electrostatic potential at the position of atom a and the second term is the charge of this atom. The potential was calculated from bond fragments as proposed previously while net charges were obtained from CNDO/2 calculations.",
author = "G. N{\'a}ray-Szab{\'o}",
year = "1984",
month = "8",
day = "8",
language = "English",
volume = "106",
pages = "4584--4589",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "American Chemical Society",
number = "16",

}

TY - JOUR

T1 - QUANTUM CHEMICAL CALCULATION OF THE ENZYME-LIGAND INTERACTION ENERGY FOR TRYPSIN INHIBITION BY BENZAMIDINES.

AU - Náray-Szabó, G.

PY - 1984/8/8

Y1 - 1984/8/8

N2 - Three-dimensional coordinates of the beta -trypsin-benzamidine complex were used to construct a quantum chemical model for the enzyme-inhibitor interaction. The model included all enzyme and benzamidinium (H//4N//2CC//6H//4X** plus ) atoms and two bound water molecules (W702 and W710) located near the binding site. Hydration was also treated by using a simple model of the first hydration sphere including four water molecules. The enzyme-inhibitor interaction energy was approximated as SIGMA V//e//n//z(r//a)qa, where the first term is the enzyme electrostatic potential at the position of atom a and the second term is the charge of this atom. The potential was calculated from bond fragments as proposed previously while net charges were obtained from CNDO/2 calculations.

AB - Three-dimensional coordinates of the beta -trypsin-benzamidine complex were used to construct a quantum chemical model for the enzyme-inhibitor interaction. The model included all enzyme and benzamidinium (H//4N//2CC//6H//4X** plus ) atoms and two bound water molecules (W702 and W710) located near the binding site. Hydration was also treated by using a simple model of the first hydration sphere including four water molecules. The enzyme-inhibitor interaction energy was approximated as SIGMA V//e//n//z(r//a)qa, where the first term is the enzyme electrostatic potential at the position of atom a and the second term is the charge of this atom. The potential was calculated from bond fragments as proposed previously while net charges were obtained from CNDO/2 calculations.

UR - http://www.scopus.com/inward/record.url?scp=0021757942&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021757942&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:0021757942

VL - 106

SP - 4584

EP - 4589

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 16

ER -