Lipid-induced conformational changes in glucagon, secretin, and vasoactive intestinal peptide

This publication has 51 references indexed in Scilit:

• Conformational changes expected in endogenous opioid peptides upon their interaction with acidic lipids
  Biochemical and Biophysical Research Communications, 1981
• Conformational properties of central nervous system myelin basic protein, β‐endorphin, and β‐lipotropin in water and in the presence of anionic lipids
  Biopolymers, 1981
• Helix End Effects in Block Copolypeptides, Proteins, and Protein-Detergent Complexes
  Macromolecules, 1980
• Brain Peptides as Neurotransmitters
  Science, 1980
• Conformational properties of the complexes formed by proteins and sodium dodecyl sulfate
  Biochemistry, 1976
• Structure of the Porcine Vasoactive Intestinal Octacosapeptide
  European Journal of Biochemistry, 1974
• Biological Activities of Synthetic Peptides Corresponding to Fragments of and to the Entire Sequence of the Vasoactive Intestinal Peptide
  Proceedings of the National Academy of Sciences, 1973
• Synthesis of secretin. IV. Secondary structure in a miniature protein
  Journal of the American Chemical Society, 1969
• Structure of Porcine Secretin. I. Degradation with Trypsin and Thrombin. Sequence of the Tryptic Peptides. The C-Terminal Residue^*
  Biochemistry, 1965
• The Amino Acid Sequence of Glucagon. V. Location of Amide Groups, Acid Degradation Studies and Summary of Sequential Evidence
  Journal of the American Chemical Society, 1957