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Physical Review. E, Statistical Physics, Plasmas, Fluids, and Related Interdisciplinary Topics|October 25, 2000
Velocity and shape selection of dendritic crystals in a forced flowTong, Beckermann, KarmaChemico-Biological Interactions|September 16, 2021
The Thr45Gly substitution in yeast alcohol dehydrogenase substantially decreases catalysis, alters pH dependencies, and disrupts the proton relay systemSuresh Pal, Bryce V PlappBiochemistry|April 11, 1995
Substitutions of isoleucine residues at the adenine binding site activate horse liver alcohol dehydrogenaseF Fan, B V PlappPhysical Review. E, Statistical, Nonlinear, and Soft Matter Physics|April 28, 2009
Phase-field modeling of dry snow metamorphismThomas U Kaempfer, Mathis PlappChemico-Biological Interactions|December 28, 2016
Inversion of substrate stereoselectivity of horse liver alcohol dehydrogenase by substitutions of Ser-48 and Phe-93Keehyuk Kim, Bryce V PlappAmerican Journal of Obstetrics and Gynecology|October 4, 2003
Fetal anemia as a response to prophylactic platelet transfusion in the management of alloimmune thrombocytopeniaJohn D Yeast, Frederick PlappBiochemistry|April 26, 2012
Atomic-resolution structures of horse liver alcohol dehydrogenase with NAD(+) and fluoroalcohols define strained Michaelis complexesBryce V Plapp, S RamaswamyBiochemistry|January 30, 2020
Substitutions of Amino Acid Residues in the Substrate Binding Site of Horse Liver Alcohol Dehydrogenase Have Small Effects on the Structures but Significantly Affect Catalysis of Hydrogen TransferKeehyuk Kim, Bryce V PlappBiochemistry|August 2, 1983
Involvement of histidine residues in the activity of horse liver alcohol dehydrogenaseM Hennecke, B V PlappPageof 72,274