An application of1H nuclear magnetic resonance to the determination of hydrophobic interactions in peptides
- 1 June 1978
- journal article
- research article
- Published by Wiley in Magnetic Resonance in Chemistry
- Vol. 11 (6) , 291-294
- https://doi.org/10.1002/mrc.1270110606
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- The Primary Structure of CollagenPublished by Elsevier ,1976
- Proton magnetic resonance assignments and conformational studies of the polypeptide antibiotic [di-N-methylleucine]gramicidin S dihydrochlorideJournal of the American Chemical Society, 1975
- Membrane proteins: Amino acid sequence and membrane penetrationJournal of Molecular Biology, 1974
- Conformational analysis of the polypeptide antibiotic telomycin by nuclear magnetic resonanceBiochemistry, 1973
- Proton magnetic resonance assignments of the polypeptide antibiotic telomycinBiochemistry, 1973
- Coacervation of α-elastin results in fiber formationBiochimica et Biophysica Acta (BBA) - Protein Structure, 1973
- Spectroscopic studies on the conformation of gramicidin A'. Proton magnetic resonance assignments, coupling constants, and hydrogen-deuterium exchangeBiochemistry, 1972
- Manifestations of the tertiary structures of proteins in high-frequency nuclear magnetic resonanceJournal of the American Chemical Society, 1967
- Nuclear magnetic resonance determination of thymine nearest neighbor baserequency ratios in deoxyribonucleic acidJournal of the American Chemical Society, 1967
- THE STRUCTURE OF WATER AND HYDROPHOBIC BONDING IN PROTEINS. III. THE THERMODYNAMIC PROPERTIES OF HYDROPHOBIC BONDS IN PROTEINS1,2The Journal of Physical Chemistry, 1962