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The Journal of Biological Chemistry|December 10, 1980
Transition state affinity jump chromatography. A double selection method for isolating catalytically active enzymes and other moleculesL Andersson, R WolfendenBiochemistry|January 15, 1985
Use of secondary isotope effects and varying pH to investigate the mode of binding of inhibitory amino aldehydes by leucine aminopeptidaseL Andersson, J MacNeela, R WolfendenBiochemistry|August 17, 1982
alpha-aminoaldehydes: transition state analogue inhibitors of leucine aminopeptidaseL Andersson, T C Isley, R WolfendenBiochemistry|February 17, 1981
Affinities of amino acid side chains for solvent waterR Wolfenden, L Andersson, P M Cullis, et al.Pharmacology & Therapeutics|November 1, 1993
Are there limits to enzyme-inhibitor binding discrimination? Inferences from the behavior of nucleoside deaminasesR WolfendenBiochemistry|January 10, 1978
Interaction of the peptide bond with solvent water: a vapor phase analysisR WolfendenBioorganic & Medicinal Chemistry|July 10, 1999
Conformational aspects of inhibitor design: enzyme-substrate interactions in the transition stateR WolfendenBiochemistry|April 16, 1996
Enzyme-substrate complexes of adenosine and cytidine deaminases: absence of accumulation of water adductsP Shih, R WolfendenBiochemistry|April 30, 1991
Analogues of intermediates in the action of pig kidney prolidaseA Radzicka, R WolfendenPageof 99