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Protein Science : a Publication of the Protein Society|December 1, 1992
Structure of the complex between trypanosomal triosephosphate isomerase and N-hydroxy-4-phosphono-butanamide: binding at the active site despite an "open" flexible loop conformationC L Verlinde, C J Witmans, T Pijning, et al.Nature|February 6, 1992
Lactose binding to heat-labile enterotoxin revealed by X-ray crystallographyT K Sixma, S E Pronk, K H Kalk, et al.FEBS Letters|February 3, 1992
X-ray studies reveal lanthanide binding sites at the A/B5 interface of E. coli heat labile enterotoxinT K Sixma, A C Terwisscha van Scheltinga, K H Kalk, et al.Infection and Immunity|December 1, 1996
Mutants of the Escherichia coli heat-labile enterotoxin with reduced ADP-ribosylation activity or no activity retain the immunogenic properties of the native holotoxinL de Haan, W R Verweij, I K Feil, et al.FEBS Letters|June 29, 1992
Heat-labile enterotoxin crystal forms with variable A/B5 orientation. Analysis of conformational flexibilityT K Sixma, A Aguirre, A C Terwisscha van Scheltinga, et al.Nature Structural Biology|January 1, 1994
The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactionsH A Schreuder, B de Boer, R Dijkema, et al.Journal of Molecular Biology|August 20, 1989
Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 A resolution. Analysis of the enzyme-substrate and enzyme-product complexesH A Schreuder, P A Prick, R K Wierenga, et al.Protein Science : a Publication of the Protein Society|July 1, 1997
Structural studies of receptor binding by cholera toxin mutantsE A Merritt, S Sarfaty, M G Jobling, et al.Structure (London, England : 1993)|June 15, 1995
Surprising leads for a cholera toxin receptor-binding antagonist: crystallographic studies of CTB mutantsE A Merritt, S Sarfaty, T T Chang, et al.Proteins|January 1, 1991
The crystal structure of the "open" and the "closed" conformation of the flexible loop of trypanosomal triosephosphate isomeraseR K Wierenga, M E Noble, J P Postma, et al.Pageof 19