Kinetic and Thermodynamic Studies of the Folding/Unfolding of a Tryptophan-Containing Mutant of Ribonuclease A

This publication has 10 references indexed in Scilit:

• The Physical Properties of Local Interactions of Tyrosine Residues in Peptides and Unfolded Proteins
  Journal of Molecular Biology, 1995
• The stability and unfolding of an IgG binding protein based upon the B domain of protein A from Staphylococcus aureus probed by tryptophan substitution and fluorescence spectroscopy
  Protein Engineering, Design and Selection, 1994
• Folding pathway of guanidine-denatured disulfide-intact wild-type and mutant bovine pancreatic ribonuclease A
  Protein Journal, 1994
• Formation of local structures in protein folding
  Accounts of Chemical Research, 1989
• THE THERMODYNAMIC STABILITY OF PROTEINS
  Annual Review of Biophysics, 1987
• The rate of interconversion between the two unfolded forms of ribonuclease A does not depend on guanidinium chloride concentration
  Journal of Molecular Biology, 1979
• [4] Vapor pressure osmometry
  Published by Elsevier ,1972
• Quantitation in Elemental Analysis
  Analytical Chemistry, 1970
• Structural Studies on Polypeptide Hormones
  Published by Elsevier ,1969
• Some spectrophotometric and polarimetric experiments with ribonuclease
  Biochimica et Biophysica Acta, 1957