Tropomyosin Paracrystals Formed by Divalent Cations
- 6 May 1966
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 152 (3723), 794-796
- https://doi.org/10.1126/science.152.3723.794
Abstract
Rabbit tropomyosin exhibits a polymorphism dependent on divalent cations and pH. Above a critical divalent cation concentration fibers with a period of about 400 angstroms are formed. Below this concentration, and near the isoelectric point, lattices are formed. Implications for the morphology and function of striated and smooth muscle are discussed.Keywords
This publication has 20 references indexed in Scilit:
- ALTERATIONS IN THE CYTOLOGIC DETAIL OF INTESTINAL SMOOTH MUSCLE CELLS IN VARIOUS STAGES OF CONTRACTIONThe Journal of cell biology, 1965
- FILAMENT LENGTHS IN STRIATED MUSCLEThe Journal of cell biology, 1963
- Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscleJournal of Molecular Biology, 1963
- X-ray diffraction evidence for α-helical coiled-coils in native muscleJournal of Molecular Biology, 1963
- The structure of F-actin and of actin filaments isolated from muscleJournal of Molecular Biology, 1963
- Evidence for the interaction between tropomyosin and actinArchives of Biochemistry and Biophysics, 1962
- Large axial spacings in striated muscleJournal of Molecular Biology, 1959
- Compound Helical Configurations of Polypeptide Chains: Structure of Proteins of the α-Keratin TypeNature, 1953
- Sub-Microscopic Localization of Minerals in Skeletal Muscle by Internal 'Micro-Incineration' within the Electron MicroscopeNature, 1949
- X-Ray Diffraction Studies on Protein Fibers. II. Feather Rachis, Porcupine Quill Tip and Clam MuscleJournal of the American Chemical Society, 1944