Investigation of labeled amino acid side-chain motion in collagen using 13C nuclear magnetic resonance
- 1 April 1980
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 138 (2) , 255-272
- https://doi.org/10.1016/0022-2836(80)90286-7
Abstract
No abstract availableThis publication has 42 references indexed in Scilit:
- Collagen Fibrils as Examples of Smectic A Biological FibresMolecular Crystals and Liquid Crystals, 1977
- X-ray diffraction by collagen tape shows that type I collagen fibrils need not have a three-dimensional latticeBiochemical and Biophysical Research Communications, 1977
- An analysis of the association of collagen based on structural modelsBiopolymers, 1976
- Observation of 13C–14N dipolar couplings in single crystals of glycineThe Journal of Chemical Physics, 1975
- Collagen polymorphism: Its origins in the amino acid sequenceJournal of Molecular Biology, 1975
- Origins and implications of the D stagger in collagenBiochemical and Biophysical Research Communications, 1974
- Packing of microfibrils in collagenJournal of Molecular Biology, 1974
- Carbon-13 magnetic resonance studies of amino acids and peptides. IIJournal of the American Chemical Society, 1970
- Nuclear Double Resonance in the Rotating FramePhysical Review B, 1962
- Theory of Line Narrowing by Double-Frequency IrradiationPhysical Review B, 1958