Dynamic Light-Scattering Evidence for the Flexibility of Native Muscle Thin Filaments
- 1 January 1980
- journal article
- research article
- Published by Elsevier in Biophysical Journal
- Vol. 29 (1), 37-47
- https://doi.org/10.1016/s0006-3495(80)85116-2
Abstract
No abstract availableThis publication has 17 references indexed in Scilit:
- Dynamics of F-actin and F-actin complexesJournal of Molecular Biology, 1974
- The helix content of tropomyosin and the interaction between tropomyosin and F-actin under various conditionsBiochimica et Biophysica Acta (BBA) - Protein Structure, 1972
- Determination of protein: A modification of the lowry method that gives a linear photometric responseAnalytical Biochemistry, 1972
- The effect of temperature on the interaction between F-actin and tropomyosinBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1971
- Dynamic study of F-actin by quasielastic scattering of laser lightJournal of Molecular Biology, 1971
- The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin.1971
- Paramyosin and the filaments of molluscan “catch” muscles: II. Native filaments: Isolation and characterizationJournal of Molecular Biology, 1971
- Use of Dimethyl Suberimidate, a Cross-Linking Reagent, in Studying the Subunit Structure of Oligomeric ProteinsProceedings of the National Academy of Sciences, 1970
- Tropomyosin: Crystal structure, polymorphism and molecular interactionsJournal of Molecular Biology, 1969
- Studies on the Interaction of F‐Actin with TropomyosinEuropean Journal of Biochemistry, 1968