The osmophobic effect: natural selection of a thermodynamic force in protein folding 1 1Edited by D. Draper

This publication has 32 references indexed in Scilit:

• The interpretation of protein structures: Estimation of static accessibility
  Published by Elsevier ,2004
• Water at Hydrophobic Surfaces: Weak Hydrogen Bonding and Strong Orientation Effects
  Science, 2001
• Monitoring the Sizes of Denatured Ensembles of Staphylococcal Nuclease Proteins: Implications Regarding m Values, Intermediates, and Thermodynamics
  Biochemistry, 1998
• Effect of Osmolytes on the Exchange Rates of Backbone Amide Protons in Proteins
  Biochemistry, 1998
• Molecular Origin of Hydration Heat Capacity Changes of Hydrophobic Solutes: Perturbation of Water Structure around Alkanes
  The Journal of Physical Chemistry B, 1997
• Modeling Unfolded States of Proteins and Peptides. II. Backbone Solvent Accessibility
  Biochemistry, 1997
• Effects of a Naturally Occurring Compatible Osmolyte on the Internal Dynamics of Ribonuclease A
  Biochemistry, 1995
• The Meaning of Hydrophobicity
  Science, 1990
• Solute compatibility with enzyme function and structure: Rationales for the selection of osmotic agents and end‐products of anaerobic metabolism in marine invertebrates
  Journal of Experimental Zoology, 1979
• A comparison of the physical chemical properties of oxidized and reduced alkylated ribonuclease
  Biochimica et Biophysica Acta, 1959