Electrostatic complementarity in molecular aggregates. Part 6. The carboxylate-imidazolium diad in Streptomyces Griseus protease A and in the 1,1′-binaphthyl-2,2′-dicarboxylic acid dihydrate- imidazole adduct

P. Nagy, J. G. Ángyán, G. Náray-Szabó

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

The electrostatic environment of the carboxylate-imidazolium diad in the active site of Streptomyces Griseus proteinase A is compared with that in a mixed crystal composed of 1,1′-binaphthyl-2,2′-dicarboxylic acid, imidazole and water. While in a previous study the geometric analogy has been stressed, it is shown in this paper that the electrostatic potential and field of the surroundings of the diad are very similar in both systems. This feature allows the crystal to be used as a simple model, relatively easily amenable to experiment, for the interpretation of various physicochemical, especially nuclear magnetic resonance spectroscopic, properties detected for serine proteases in solution.

Original languageEnglish
Pages (from-to)169-176
Number of pages8
JournalJournal of Molecular Structure: THEOCHEM
Volume149
Issue number1-2
DOIs
Publication statusPublished - 1987

Fingerprint

Dicarboxylic Acids
protease
dicarboxylic acids
Static Electricity
imidazoles
carboxylates
adducts
Electrostatics
electrostatics
Crystals
Acids
mixed crystals
Serine Proteases
Catalytic Domain
Magnetic Resonance Spectroscopy
Nuclear magnetic resonance
nuclear magnetic resonance
Water
water
crystals

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Computational Theory and Mathematics
  • Atomic and Molecular Physics, and Optics

Cite this

@article{ef1b83460d0b4e2a8b7fcedd10bcde75,
title = "Electrostatic complementarity in molecular aggregates. Part 6. The carboxylate-imidazolium diad in Streptomyces Griseus protease A and in the 1,1′-binaphthyl-2,2′-dicarboxylic acid dihydrate- imidazole adduct",
abstract = "The electrostatic environment of the carboxylate-imidazolium diad in the active site of Streptomyces Griseus proteinase A is compared with that in a mixed crystal composed of 1,1′-binaphthyl-2,2′-dicarboxylic acid, imidazole and water. While in a previous study the geometric analogy has been stressed, it is shown in this paper that the electrostatic potential and field of the surroundings of the diad are very similar in both systems. This feature allows the crystal to be used as a simple model, relatively easily amenable to experiment, for the interpretation of various physicochemical, especially nuclear magnetic resonance spectroscopic, properties detected for serine proteases in solution.",
author = "P. Nagy and {\'A}ngy{\'a}n, {J. G.} and G. N{\'a}ray-Szab{\'o}",
year = "1987",
doi = "10.1016/0166-1280(87)80059-3",
language = "English",
volume = "149",
pages = "169--176",
journal = "Computational and Theoretical Chemistry",
issn = "2210-271X",
publisher = "Elsevier BV",
number = "1-2",

}

TY - JOUR

T1 - Electrostatic complementarity in molecular aggregates. Part 6. The carboxylate-imidazolium diad in Streptomyces Griseus protease A and in the 1,1′-binaphthyl-2,2′-dicarboxylic acid dihydrate- imidazole adduct

AU - Nagy, P.

AU - Ángyán, J. G.

AU - Náray-Szabó, G.

PY - 1987

Y1 - 1987

N2 - The electrostatic environment of the carboxylate-imidazolium diad in the active site of Streptomyces Griseus proteinase A is compared with that in a mixed crystal composed of 1,1′-binaphthyl-2,2′-dicarboxylic acid, imidazole and water. While in a previous study the geometric analogy has been stressed, it is shown in this paper that the electrostatic potential and field of the surroundings of the diad are very similar in both systems. This feature allows the crystal to be used as a simple model, relatively easily amenable to experiment, for the interpretation of various physicochemical, especially nuclear magnetic resonance spectroscopic, properties detected for serine proteases in solution.

AB - The electrostatic environment of the carboxylate-imidazolium diad in the active site of Streptomyces Griseus proteinase A is compared with that in a mixed crystal composed of 1,1′-binaphthyl-2,2′-dicarboxylic acid, imidazole and water. While in a previous study the geometric analogy has been stressed, it is shown in this paper that the electrostatic potential and field of the surroundings of the diad are very similar in both systems. This feature allows the crystal to be used as a simple model, relatively easily amenable to experiment, for the interpretation of various physicochemical, especially nuclear magnetic resonance spectroscopic, properties detected for serine proteases in solution.

UR - http://www.scopus.com/inward/record.url?scp=45949121790&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=45949121790&partnerID=8YFLogxK

U2 - 10.1016/0166-1280(87)80059-3

DO - 10.1016/0166-1280(87)80059-3

M3 - Article

AN - SCOPUS:45949121790

VL - 149

SP - 169

EP - 176

JO - Computational and Theoretical Chemistry

JF - Computational and Theoretical Chemistry

SN - 2210-271X

IS - 1-2

ER -