Infrared Absorption Study of Peptide Fragments of Human Hemoglobin α-Chain (123–136) in the Solid State
- 1 July 1987
- journal article
- Published by Oxford University Press (OUP) in Bulletin of the Chemical Society of Japan
- Vol. 60 (7), 2445-2451
- https://doi.org/10.1246/bcsj.60.2445
Abstract
No abstract availableThis publication has 21 references indexed in Scilit:
- The Ability of the Proline Residue to Promote Successive-Intramolecular Hydrogen Bonds in OligopeptidesBulletin of the Chemical Society of Japan, 1986
- Infrared Absorption Study of Human Proinsulin C-Peptide Fragments in DichloromethaneBulletin of the Chemical Society of Japan, 1986
- Infrared Absorption Study of Human Proinsulin C-Peptide Fragments in the Solid StateBulletin of the Chemical Society of Japan, 1986
- Critical Peptide Size for Insolubility Caused by a β-Sheet Aggregation and Solubility Improvement in Hydrophobic Peptides by Replacement of Alanine Residues with α-Aminoisobutyric Acid ResiduesBulletin of the Chemical Society of Japan, 1985
- Syntheses and properties of tertiary peptide bond containing polypeptides. 7. Conformational studies of sequential polypeptides containing the Pro-Pro sequence by carbon-13 and proton NMRMacromolecules, 1985
- Syntheses and properties of tertiary peptide bond containing polypeptides. 6. Conformational studies of oligopeptides containing the Pro-Pro sequence by carbon-13 and proton NMRMacromolecules, 1985
- Conformation of sequential peptides containing proline residuesInternational Journal of Peptide and Protein Research, 1984
- Structure of horse carbonmonoxyhaemoglobinJournal of Molecular Biology, 1976
- Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteinsBiochemistry, 1974
- The Infrared Spectra of Polypeptides in Various Conformations: Amide I and II Bands1Journal of the American Chemical Society, 1961