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Conformational preferences of the substrates of lactate dehydrogenase.

dc.contributor.authorSchmidt, Rebecca
dc.contributor.authorGready, Jill
dc.date.accessioned2015-12-08T22:41:57Z
dc.date.issued2000
dc.date.updated2015-12-08T10:31:44Z
dc.description.abstractThe substrates of lactate dehydrogenase (pyruvate and lactate) as well as an inhibitor (oxamate) are characterized using ab initio methods employing the basis sets 6-31 +G(d) and 6-31 +G(d, p) at both RHF and MP2 levels. The first aim of these studies is
dc.identifier.issn0022-2860
dc.identifier.urihttp://hdl.handle.net/1885/36875
dc.publisherElsevier
dc.sourceJournal of Molecular Structure
dc.subjectKeywords: carbon; carbonyl derivative; carboxyl group; lactate dehydrogenase; lactic acid; methyl group; oxamic acid; oxygen; pyruvic acid; accuracy; article; calculation; chemical structure; controlled study; crystal structure; energy; enthalpy; enzyme active site Ab initio; Conformer; Lactate; Lactate dehydrogenase; Oxamate; Pyruvate; Semiempirical
dc.titleConformational preferences of the substrates of lactate dehydrogenase.
dc.typeJournal article
local.bibliographicCitation.lastpage112
local.bibliographicCitation.startpage101
local.contributor.affiliationSchmidt, Rebecca, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationGready, Jill, College of Medicine, Biology and Environment, ANU
local.contributor.authoruidSchmidt, Rebecca, u9604481
local.contributor.authoruidGready, Jill, u9508375
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.absfor030499 - Medicinal and Biomolecular Chemistry not elsewhere classified
local.identifier.absfor030701 - Quantum Chemistry
local.identifier.ariespublicationMigratedxPub142
local.identifier.citationvolume498
local.identifier.doi10.1016/S0166-1280(99)00252-3
local.identifier.scopusID2-s2.0-0034723984
local.type.statusPublished Version

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