Osmolytes Stabilize Ribonuclease S by Stabilizing Its Fragments S Protein and S Peptide to Compact Folding-competent States

This publication has 58 references indexed in Scilit:

• Native-state hydrogen-exchange studies of a fragment complex can provide structural information about the isolated fragments
  Proceedings of the National Academy of Sciences, 1999
• Mechanism of the stabilization of ribonuclease a by sorbitol: Preferential hydration is greater for the denatured than for the native protein
  Protein Science, 1997
• The Peptide Backbone Plays a Dominant Role in Protein Stabilization by Naturally Occurring Osmolytes
  Biochemistry, 1995
• An osmolyte effect on the heat capacity change for protein folding
  Biochemistry, 1995
• Why do some organisms use a urea-methylamine mixture as osmolyte? Thermodynamic compensation of urea and trimethylamine N-oxide interactions with protein
  Biochemistry, 1994
• Refinement of the crystal structure of ribonuclease S. Comparison with and between the various ribonuclease A structures
  Biochemistry, 1992
• Increased thermal stability of proteins in the presence of naturally occurring osmolytes
  Biochemistry, 1992
• The stabilization of proteins by osmolytes
  Biophysical Journal, 1985
• Living with Water Stress: Evolution of Osmolyte Systems
  Science, 1982
• Counteraction of urea destabilization of protein structure by methylamine osmoregulatory compounds of elasmobranch fishes
  Biochemical Journal, 1979