Heat denaturation and cold denaturation of Escherichia coli RNase HI investigated by circular dichroism

This publication has 13 references indexed in Scilit:

• Equilibrium unfolding of Escherichia coli ribonuclease H: Characterization of a partially folded state
  Protein Science, 1994
• Hydration and heat stability effects on protein unfolding
  Progress in Biophysics and Molecular Biology, 1993
• Complete assignments of magnetic resonances of ribonuclease H from Escherichia coli by double- and triple-resonance 2D and 3D NMR spectroscopies
  Biochemistry, 1993
• pH-Dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions
  Journal of Biotechnology, 1993
• Structural details of ribonuclease H from Escherichia coli as refined to an atomic resolution
  Journal of Molecular Biology, 1992
• Assignments of backbone proton, carbon-13, and nitrogen-15 resonances and secondary structure of ribonuclease H from Escherichia coli by heteronuclear three-dimensional NMR spectroscopy
  Biochemistry, 1991
• Role of cysteine residues in ribonuclease H from Escherichia coli. Site-directed mutagenesis and chemical modification
  Biochemical Journal, 1990
• Structure of Ribonuclease H Phased at 2 Å Resolution by MAD Analysis of the Selenomethionyl Protein
  Science, 1990
• Cold Denaturation of Protein
  Critical Reviews in Biochemistry and Molecular Biology, 1990
• d-Pantolactone as a circular dichromism (CD) calibration
  Analytical Biochemistry, 1975