A HIGH RESOLUTION 13C NMR STUDY OF SILK FIBROIN IN SOLID STATE BY THE CROSS POLARIZATION-MAGIC ANGLE SPINNING METHOD: CONFORMATIONAL CHARACTERIZATION UTILIZING CONFORMATION-DEPENDENT 13C CHEMICAL SHIFTS
- 5 April 1983
- journal article
- Published by Oxford University Press (OUP) in Chemistry Letters
- Vol. 12 (4) , 427-430
- https://doi.org/10.1246/cl.1983.427
Abstract
No abstract availableThis publication has 16 references indexed in Scilit:
- Solid State NMR of Linear and Cyclic PeptidesPublished by American Chemical Society (ACS) ,1982
- A 13C Nuclear Magnetic Resonance Study of Histone H1 in 2-ChIoroethanol and Aqueous Solutions. Identification of Peaks Characteristic of Secondary Folding1The Journal of Biochemistry, 1982
- Observation of conformationally distinct proline residues in two cyclic peptides by solid-state nuclear magnetic resonanceJournal of the American Chemical Society, 1981
- Comparison of protein structures by high resolution solid state and solution NMRFEBS Letters, 1980
- Detection of individual carbon resonances in solid proteinsJournal of the American Chemical Society, 1979
- Physical properties and structure of silk. VI. Conformational changes in silk fibroin induced by immersion in water at 2 to 130°cJournal of Polymer Science: Polymer Physics Edition, 1979
- Carbon-13-NMR of peptides and proteinsProgress in Nuclear Magnetic Resonance Spectroscopy, 1978
- Carbon-13 nuclear magnetic resonance of polymers spinning at the magic angleJournal of the American Chemical Society, 1976
- Proton-enhanced NMR of dilute spins in solidsThe Journal of Chemical Physics, 1973
- The narrowing of NMR spectra of solids by high-speed specimen rotation and the resolution of chemical shift and spin multiplet structures for solidsProgress in Nuclear Magnetic Resonance Spectroscopy, 1971