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Biophysical Chemistry|August 1, 1988
On the relevance of non-random polypeptide conformations for protein foldingT E CreightonProceedings of the National Academy of Sciences of the United States of America|July 1, 1988
Toward a better understanding of protein folding pathwaysT E CreightonBiochemistry|October 3, 1995
Effects of trifluoroethanol on the conformations of peptides representing the entire sequence of bovine pancreatic trypsin inhibitorJ Kemmink, T E CreightonBiochemistry|May 3, 1994
Effects of DsbA on the disulfide folding of bovine pancreatic trypsin inhibitor and alpha-lactalbuminA Zapun, T E CreightonBiochimica Et Biophysica Acta|March 4, 1982
Effect on protein stability of reversing the charge on amino groupsM Hollecker, T E CreightonJournal of Molecular Biology|November 10, 1995
Ionisation of cysteine residues at the termini of model alpha-helical peptides. Relevance to unusual thiol pKa values in proteins of the thioredoxin familyT Kortemme, T E CreightonJournal of Molecular Biology|January 20, 1995
The physical properties of local interactions of tyrosine residues in peptides and unfolded proteinsJ Kemmink, T E CreightonBiochemistry|June 25, 1996
On the reactivity and ionization of the active site cysteine residues of Escherichia coli thioredoxinN Takahashi, T E CreightonJournal of Molecular Biology|December 5, 1993
Local conformations of peptides representing the entire sequence of bovine pancreatic trypsin inhibitor and their roles in foldingJ Kemmink, T E CreightonJournal of Molecular Biology|October 7, 1994
Electrophoretic characterization of the denatured states of staphylococcal nucleaseT E Creighton, D ShortlePageof 9