Bovine trypsin inhibitor mutants

K. D. Wittrup. Secretion effidency in Saccharomyces cerevisiae of bovine pancreatic trypsin inhibitor mutants lacking disulfide bonds is correlated with thermodynamic stability. Biochemistry (1998) 37(5) 1264-73. 

Sreerama, N., Manning, M.C., Powers, M.E., Zhang. J.X., Goldenberg, D.P., and Woody, R.W. 1999a. Tyrosine, phenylalanine, and disulfide contributions to the circular dichroism of proteins Circular dichroism spectra of wild-type and mutant bovine pancreatic trypsin inhibitor. Biochemistry 38 10814-10822. 

Y. Liu, K. Breslauer, and S. Anderson, Designing Out Disulfide Bonds Thermodynamic Properties of 30-51 Cystine Substitution Mutants of Bovine Pancreatic Trypsin Inhibitor , Biochemistry, 36, 5323-5335 (1997). 

Grzesiak A, Krokoszynska I, Krowarsch D, Buczek O, Dadlez M, Otlewski J. Inhibition of six serine proteinases of the human coagulation system by mutants of bovine pancreatic trypsin inhibitor. J Biol Chem 2000 275 33346-33352. 

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