Identification of the divalent metal ion binding domain of myosin regulatory light chains using spin-labelling techniques
- 1 July 1980
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 140 (3), 411-433
- https://doi.org/10.1016/0022-2836(80)90392-7
Abstract
No abstract availableThis publication has 30 references indexed in Scilit:
- Characterization of homologous divalent metal ion binding sites of vertebrate and molluscan myosins using electron paramagnetic resonance spectroscopyJournal of Molecular Biology, 1979
- Spectroscopic studies on invertebrate myosins and light chainsBiochemistry, 1978
- Interaction of spin labels with transition metalsCoordination Chemistry Reviews, 1978
- Interaction of skeletal myosin light chains with calcium ionsBiochemistry, 1978
- The significance of the slow dissociation of divalent metal ions from myosin ‘regulatory’ light chainsFEBS Letters, 1977
- The location of the divalent metal binding sites and the light chain subunits of vertebrate myosinBiochemistry, 1977
- Calcium binding regions of myosin ‘Regulatory’ light chainsFEBS Letters, 1976
- Homology of myosin DTNB light chain with alkali light chains, troponin C and parvalbuminNature, 1976
- Cyanylation of sulfhydryl groups by 2-nitro-5-thiocyanobenzoic acid. High-yield modification and cleavage of peptides at cysteine residuesBiochemistry, 1974
- Strategy and tactics in protein chemistryBiochemical Journal, 1970