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Journal of Molecular Biology|August 5, 1983
Evolutionary conservation and variation of protein folding pathways. Two protease inhibitor homologues from black mamba venomM Hollecker, T E CreightonBiochemistry|April 13, 1993
Pathway of disulfide-coupled unfolding and refolding of bovine alpha-lactalbuminJ J Ewbank, T E CreightonBiochemistry|March 21, 1995
Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomeraseN J Darby, T E CreightonAnalytical Biochemistry|April 1, 1984
Gel electrophoresis in studies of protein conformation and foldingD P Goldenberg, T E CreightonBiochemistry|May 17, 1994
Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivoJ W Nelson, T E CreightonBiochemistry|September 19, 1995
Functional properties of the individual thioredoxin-like domains of protein disulfide isomeraseN J Darby, T E CreightonJournal of Molecular Biology|August 5, 1993
Dissecting the disulphide-coupled folding pathway of bovine pancreatic trypsin inhibitor. Forming the first disulphide bonds in analogues of the reduced proteinN J Darby, T E CreightonJournal of Molecular Biology|April 5, 1983
Circular and circularly permuted forms of bovine pancreatic trypsin inhibitorD P Goldenberg, T E CreightonBiochemistry|December 26, 1995
Characterization of the active site cysteine residues of the thioredoxin-like domains of protein disulfide isomeraseN J Darby, T E CreightonTrends in Biochemical Sciences|August 1, 1989
Functional evolutionary divergence of proteolytic enzymes and their inhibitorsT E Creighton, N J DarbyPageof 9