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Journal of Molecular Biology|November 20, 1991
(14-38, 30-51) double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: a two-dimensional 1H nuclear magnetic resonance studyC P van Mierlo, N J Darby, D Neuhaus, et al.Journal of Molecular Biology|November 20, 1991
Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitorC P van Mierlo, N J Darby, D Neuhaus, et al.The EMBO Journal|July 1, 1994
Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha-lactalbuminM K Hayer-Hartl, J J Ewbank, T E Creighton, et al.Protein Science : a Publication of the Protein Society|December 1, 1995
Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomeraseJ Kemmink, N J Darby, K Dijkstra, et al.Medical Care|October 1, 1987
Self-care and self-medication. An evaluation of individuals' health care decisionsI F Wilkinson, D N Darby, A MantBiotelemetry and Patient Monitoring|January 1, 1980
Assessment of the diagnostic value of 24-hour ambulatory electrocardiographic monitoringD E Ward, A J Camm, N DarbyJournal of Molecular Biology|January 21, 1994
1H NMR analysis of the partly-folded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitorC P van Mierlo, J Kemmink, D Neuhaus, et al.Journal of Molecular Biology|February 20, 1993
Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurementsC P van Mierlo, N J Darby, J Keeler, et al.Acta Crystallographica. Section D, Biological Crystallography|November 1, 1996
Crystallization of DsbC, the disulfide bond isomerase of Escherichia coliV Rybin, A Zapun, A Törrönen, et al.Journal of Molecular Biology|April 20, 1992
Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitorN J Darby, C P van Mierlo, G H Scott, et al.Pageof 9