Transition-state structural refinement with GRACE and CHARMM: Realistic modelling of lactate dehydrogenase using a combined quantum/classical method

Vicente Moliner; Alexander J. Turner; Ian H. Williams

doi:10.1039/a702600e

Transition-state structural refinement with GRACE and CHARMM: Realistic modelling of lactate dehydrogenase using a combined quantum/classical method

Vicente Moliner, Alexander J. Turner, Ian H. Williams

Department of Chemistry

Research output: Contribution to journal › Article › peer-review

71 Citations (SciVal)

Abstract

A transition structure for reduction of pyruvate catalysed by lactate dehydrogenase is refined and characterised in hybrid quantum mechanical/molecular mechanical (AM1/CHARMM) calculations involving a fully flexible active-site region by means of a novel procedure (GRACE), and is remarkably similar to that calculated in vacuo.

Original language	English
Pages (from-to)	1271-1272
Number of pages	2
Journal	Chemical Communications
Volume	1997
Issue number	14
DOIs	https://doi.org/10.1039/a702600e
Publication status	Published - 1 Jan 1997

ASJC Scopus subject areas

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
General Chemistry
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

Access to Document

10.1039/a702600e

Cite this

@article{ac21cf2b38b547159312deebb98784b3,

title = "Transition-state structural refinement with GRACE and CHARMM: Realistic modelling of lactate dehydrogenase using a combined quantum/classical method",

abstract = "A transition structure for reduction of pyruvate catalysed by lactate dehydrogenase is refined and characterised in hybrid quantum mechanical/molecular mechanical (AM1/CHARMM) calculations involving a fully flexible active-site region by means of a novel procedure (GRACE), and is remarkably similar to that calculated in vacuo.",

author = "Vicente Moliner and Turner, {Alexander J.} and Williams, {Ian H.}",

year = "1997",

month = jan,

day = "1",

doi = "10.1039/a702600e",

language = "English",

volume = "1997",

pages = "1271--1272",

journal = "Chemical Communications",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

number = "14",

}

TY - JOUR

T1 - Transition-state structural refinement with GRACE and CHARMM

T2 - Realistic modelling of lactate dehydrogenase using a combined quantum/classical method

AU - Moliner, Vicente

AU - Turner, Alexander J.

AU - Williams, Ian H.

PY - 1997/1/1

Y1 - 1997/1/1

N2 - A transition structure for reduction of pyruvate catalysed by lactate dehydrogenase is refined and characterised in hybrid quantum mechanical/molecular mechanical (AM1/CHARMM) calculations involving a fully flexible active-site region by means of a novel procedure (GRACE), and is remarkably similar to that calculated in vacuo.

AB - A transition structure for reduction of pyruvate catalysed by lactate dehydrogenase is refined and characterised in hybrid quantum mechanical/molecular mechanical (AM1/CHARMM) calculations involving a fully flexible active-site region by means of a novel procedure (GRACE), and is remarkably similar to that calculated in vacuo.

UR - http://www.scopus.com/inward/record.url?scp=0002709949&partnerID=8YFLogxK

U2 - 10.1039/a702600e

DO - 10.1039/a702600e

M3 - Article

AN - SCOPUS:0002709949

SN - 1359-7345

VL - 1997

SP - 1271

EP - 1272

JO - Chemical Communications

JF - Chemical Communications

IS - 14

ER -

Transition-state structural refinement with GRACE and CHARMM: Realistic modelling of lactate dehydrogenase using a combined quantum/classical method

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this