Postulates for protein (hydrophobic) folding and function

This publication has 32 references indexed in Scilit:

• Probing the structure of folding intermediates
  Current Opinion in Structural Biology, 1994
• Nanometric design of extraordinary hydrophobic‐induced pKa shifts for aspartic acid: Relevance to protein mechanisms
  Biopolymers, 1994
• Relative Significance of Electrostatic‐ and Hydrophobic‐Induced pK_a Shifts in a Model Protein: The Aspartic Acid Residue
  Angewandte Chemie International Edition in English, 1993
• Solvent deuteration enhancement of hydrophobicity: DSC study of the inverse temperature transition of elastin-based polypeptides
  The Journal of Physical Chemistry, 1991
• Differential scanning calorimetry studies of NaCl effect on the inverse temperature transition of some elastin‐based polytetra‐, polypenta‐, and polynonapeptides
  Biopolymers, 1991
• Entropic elastomeric force in protein structure/function
  International Journal of Quantum Chemistry, 1987
• Temperature-correlated force and structure development in elastomeric polypeptides: The Ile1 analog of the polypentapeptide of elastin
  Biopolymers, 1986
• Water and proteins. II. The location and dynamics of water in protein systems and its relation to their stability and properties
  Advances in Biophysics, 1983
• A Method for Predicting Nucleation Sites for Protein Folding Based on Hydrophobic Contacts
  Macromolecules, 1978
• Apparent Molal Heat Capacities of Amino Acids and Other Organic Compounds
  Journal of the American Chemical Society, 1935