Hydrogen bonding interactions between glutamine and asparagine in α-helical peptides 1 1Edited by A. R. Fersht

This publication has 57 references indexed in Scilit:

• Energetic contribution of side chain hydrogen bonding to the stability of staphylococcal nuclease
  Biochemistry, 1995
• Stability of α-Helices
  Published by Elsevier ,1995
• Helix propensities of the amino acids measured in alanine‐based peptides without helix‐stabilizing side‐chain interactions
  Protein Science, 1994
• Contribution of Buried Hydrogen Bonds to Protein Stability The Crystal Structures of Two Barnase Mutants
  Journal of Molecular Biology, 1993
• Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensities
  Biochemistry, 1993
• The (i,i+4) Phe-His Interaction Studied in an Alanine-based α-Helix
  Journal of Molecular Biology, 1993
• Large differences in the helix propensities of alanine and glycine
  Nature, 1991
• pH-Induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme
  Biochemistry, 1990
• Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme
  Nature, 1987
• Determination of the helix and β form of proteins in aqueous solution by circular dichroism
  Biochemistry, 1974