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The Journal of Biological Chemistry|April 10, 1985
The refinement and the structure of the dimer of alpha-chymotrypsin at 1.67-A resolutionR A Blevins, A TulinskyBiochemistry|October 5, 1976
The folding and quaternary structure of trimeric 2-keto-3-deoxy-6-phosphogluconic aldolase at 3.5-A resolutionI M Mavridis, A TulinskyActa Crystallographica. Section D, Biological Crystallography|July 1, 1995
Active-site mimetic inhibition of thrombinI I Mathews, A TulinskyThe Journal of Biological Chemistry|June 5, 1987
Structure of a tetrahedral transition state complex of alpha-chymotrypsin dimer at 1.8-A resolutionA Tulinsky, R A BlevinsBiochemistry|July 15, 1986
Three-dimensional structure of the kringle sequence: structure of prothrombin fragment 1C H Park, A TulinskyActa Crystallographica. Section D, Biological Crystallography|March 31, 2000
Structure of the Ser195Ala mutant of human alpha--thrombin complexed with fibrinopeptide A(7--16): evidence for residual catalytic activityR Krishnan, J E Sadler, A TulinskyThe Journal of Biological Chemistry|September 5, 1985
The structure of prothrombin fragment 1 at 3.5-A resolutionA Tulinsky, C H Park, T J RydelBiochemistry|December 20, 1994
Functions of individual gamma-carboxyglutamic acid (Gla) residues of human protein c. Determination of functionally nonessential Gla residues and correlations with their mode of binding to calciumW T Christiansen, A Tulinsky, F J CastellinoJournal of Molecular Biology|February 2, 1999
Structure of extracellular tissue factor complexed with factor VIIa inhibited with a BPTI mutantE Zhang, R St Charles, A TulinskyThe Journal of Biological Chemistry|February 25, 1978
Expression of functionality of alpha-chymotrypsin. An alternate binding mode in the substrate specificity siteA Tulinsky, I Mavridis, R F MannPageof 50