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Biochemistry|July 28, 1992
Unfolding of trp repressor studied using fluorescence spectroscopic techniquesT Fernando, C A RoyerAnalytical Biochemistry|April 1, 1993
Improvements in the numerical analysis of thermodynamic data from biomolecular complexesC A RoyerBrazilian Journal of Medical and Biological Research = Revista Brasileira De Pesquisas Medicas E Biologicas|August 6, 2005
Insights into the role of hydration in protein structure and stability obtained through hydrostatic pressure studiesC A RoyerBiophysical Journal|September 1, 1992
Investigation of the structural determinants of the intrinsic fluorescence emission of the trp repressor using single tryptophan mutantsC A RoyerBiochemistry|August 3, 1993
Fluorescence anisotropy assays implicate protein-protein interactions in regulating trp repressor DNA bindingV LeTilly, C A RoyerJournal of Molecular Biology|January 7, 2000
The basis for the super-repressor phenotypes of the AV77 and EK18 mutants of trp repressorA O Grillo, C A RoyerProtein Science : a Publication of the Protein Society|April 1, 1997
The kinetic basis for the stabilization of staphylococcal nuclease by xyloseK J Frye, C A RoyerProtein Science : a Publication of the Protein Society|October 29, 1998
Probing the contribution of internal cavities to the volume change of protein unfolding under pressureK J Frye, C A RoyerJournal of Molecular Biology|October 20, 1995
Evidence for coupling of folding and function in trp repressor: physical characterization of the superrepressor mutant AV77R J Reedstrom, C A RoyerPageof 13