Lipid-induced conformational changes in glucagon, secretin, and vasoactive intestinal peptide
- 1 June 1982
- journal article
- research article
- Published by Wiley in Peptide Science
- Vol. 21 (6), 1217-1228
- https://doi.org/10.1002/bip.360210615
Abstract
No abstract availableThis publication has 51 references indexed in Scilit:
- Conformational changes expected in endogenous opioid peptides upon their interaction with acidic lipidsBiochemical 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 lipidsPeptide Science, 1981
- Helix End Effects in Block Copolypeptides, Proteins, and Protein-Detergent ComplexesMacromolecules, 1980
- Brain Peptides as NeurotransmittersScience, 1980
- Conformational properties of the complexes formed by proteins and sodium dodecyl sulfateBiochemistry, 1976
- Structure of the Porcine Vasoactive Intestinal OctacosapeptideEuropean Journal of Biochemistry, 1974
- Biological Activities of Synthetic Peptides Corresponding to Fragments of and to the Entire Sequence of the Vasoactive Intestinal PeptideProceedings of the National Academy of Sciences of the United States of America, 1973
- Synthesis of secretin. IV. Secondary structure in a miniature proteinJournal 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 EvidenceJournal of the American Chemical Society, 1957