Schmidt, RebeccaGready, Jill2015-12-080022-2860http://hdl.handle.net/1885/36875The 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 isKeywords: 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; SemiempiricalConformational preferences of the substrates of lactate dehydrogenase.200010.1016/S0166-1280(99)00252-32015-12-08