A preferred conformation in the vasoactive intestinal peptide (VIP). Molecular architecture of gastrointestinal hormones
- 1 June 1974
- journal article
- Published by Elsevier BV in Bioorganic Chemistry
- Vol. 3 (2), 133-140
- https://doi.org/10.1016/0045-2068(74)90037-6
Abstract
No abstract availableThis publication has 16 references indexed in Scilit:
- Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersionBiochemistry, 1972
- Isolation from Porcine‐Intestinal Wall of a Vasoactive Octacosapeptide Related to Secretin and to GlucagonEuropean Journal of Biochemistry, 1972
- Secretin. V. Solvent effects and conformational freedomJournal of the American Chemical Society, 1972
- Polypeptide with Broad Biological Activity: Isolation from Small IntestineScience, 1970
- Protein-solvent interactions and protein conformationAccounts of Chemical Research, 1970
- Statistical analysis of the distribution of amino acid residues among helical and non-helical regions in globular proteinsJournal of Molecular Biology, 1969
- Synthesis of secretin. IV. Secondary structure in a miniature proteinJournal of the American Chemical Society, 1969
- The helix–coil transition of poly‐L‐lysine in methanol–water solvent mixturesPeptide Science, 1968
- A Conformational Study of GlucagonEuropean Journal of Biochemistry, 1968
- The Effect of Protein Denaturants on the Stability of the α Helix1Journal of the American Chemical Society, 1966