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Nature|August 7, 1980
A conformational isomer of bovine pancreatic trypsin inhibitor protein produced by refoldingD J States, C M Dobson, M Karplus, et al.Australian Clinical Review|January 1, 1992
ACHS surveyor recommendations: recent trends in the accident and emergency serviceP E Holt, D N DarbyJournal of Molecular Biology|June 2, 1995
Refolding of bovine pancreatic trypsin inhibitor via non-native disulphide intermediatesN J Darby, P E Morin, G Talbo, et al.European Journal of Biochemistry|October 15, 1985
Comparative studies of conformation and internal mobility in native and circular basic pancreatic trypsin inhibitor by 1H nuclear magnetic resonance in solutionW J Chazin, D P Goldenberg, T E Creighton, et al.Proteins|September 1, 1992
Folding in vitro of bovine pancreatic trypsin inhibitor in the presence of proteins of the endoplasmic reticulumA Zapun, T E Creighton, P J Rowling, et al.Biochemistry|February 3, 1981
Circular dichroism, Raman spectroscopy, and gel filtration of trapped folding intermediates of ribonucleaseA Galat, T E Creighton, R C Lord, et al.Journal of Molecular Biology|June 5, 1987
Conformations of intermediates in the folding of the pancreatic trypsin inhibitorD J States, T E Creighton, C M Dobson, et al.Biochemistry|June 18, 1996
Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopyJ Kemmink, N J Darby, K Dijkstra, et al.Current Biology : CB|April 1, 1997
The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modulesJ Kemmink, N J Darby, K Dijkstra, et al.Journal of Molecular Biology|March 5, 1993
Local structure due to an aromatic-amide interaction observed by 1H-nuclear magnetic resonance spectroscopy in peptides related to the N terminus of bovine pancreatic trypsin inhibitorJ Kemmink, C P van Mierlo, R M Scheek, et al.Pageof 9