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Biochimica Et Biophysica Acta|October 16, 2007
Examination of the mechanism and energetic contribution of leaving group activation in the purine-specific nucleoside hydrolase from Trypanosoma vivaxJohn N Barlow, Jan SteyaertBiochemistry|March 13, 2014
Inhibition of ligand exchange kinetics via active-site trapping with an antibody fragmentDavid Oyen, Jan Steyaert, John N BarlowBiochimica Et Biophysica Acta|April 8, 2009
Substrate-dependent modulation of enzyme activity by allosteric effector antibodiesJohn N Barlow, Katja Conrath, Jan SteyaertJournal of Molecular Biology|January 18, 2011
Constraining enzyme conformational change by an antibody leads to hyperbolic inhibitionDavid Oyen, Vasundara Srinivasan, Jan Steyaert, et al.Biochemistry|July 27, 2006
Multiple transients in the pre-steady-state of nucleoside hydrolase reveal complex substrate binding, product base release, and two apparent rates of chemistryAn Vandemeulebroucke, Wim Versées, Jan Steyaert, et al.Biochimica Et Biophysica Acta|August 6, 2013
Mechanistic analysis of allosteric and non-allosteric effects arising from nanobody binding to two epitopes of the dihydrofolate reductase of Escherichia coliDavid Oyen, Rainer Wechselberger, Vasundara Srinivasan, et al.The Journal of Biological Chemistry|December 19, 2001
The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical stepMiryam Asuncion, Wulf Blankenfeldt, John N Barlow, et al.Pageof 1