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Biochemistry|January 11, 1994
Single peptide bond hydrolysis/resynthesis in squash inhibitors of serine proteinases. 1. Kinetics and thermodynamics of the interaction between squash inhibitors and bovine beta-trypsinJ Otlewski, T ZbyrytBiological Chemistry Hoppe-Seyler|April 1, 1991
Interaction between squash inhibitors and bovine trypsinogenT Zbyryt, J OtlewskiBiological Chemistry Hoppe-Seyler|July 1, 1990
Inhibition of serine proteinases by squash inhibitorsJ Otlewski, T Zbyryt, I Krokoszyńska, et al.Biochemistry|January 11, 1994
Single peptide bond hydrolysis/resynthesis in squash inhibitors of serine proteinases. 2. Limited proteolysis of Curcurbita maxima trypsin inhibitor I by pepsinJ Otlewski, T Zbyryt, M Dryjański, et al.Biological Chemistry Hoppe-Seyler|October 1, 1992
New analogues of Cucurbita maxima trypsin inhibitor III (CMTI III) with simplified structureK Rolka, G Kupryszewski, J Rózycki, et al.Journal of Molecular Biology|March 8, 1996
Thermodynamic stability effects of single peptide bond hydrolysis in protein inhibitors of serine proteinasesI Krokoszyńska, J OtlewskiEuropean Journal of Biochemistry|August 1, 1994
Denaturation of free and complexed bovine trypsinogen with the calcium ion, dipeptide Ile-Val and basic pancreatic trypsin inhibitor (Kunitz)G Bulaj, J OtlewskiActa Biochimica Polonica|January 1, 1997
Structural and energetic aspects of protein-protein recognitionJ Otlewski, W ApostolukProtein Science : a Publication of the Protein Society|March 29, 2001
Amino-acid substitutions at the fully exposed P1 site of bovine pancreatic trypsin inhibitor affect its stabilityD Krowarsch, J OtlewskiJournal of Molecular Biology|April 7, 1995
Ligand-induced changes in the conformational stability of bovine trypsinogen and their implications for the protein functionG Bulaj, J OtlewskiPageof 7