Prediction of the secondary structure of myosin light chains from comparison of homologous sequences. Implications for the interaction between myosin heavy and light chains
- 1 July 1989
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 996 (3), 199-208
- https://doi.org/10.1016/0167-4838(89)90248-3
Abstract
No abstract availableKeywords
This publication has 73 references indexed in Scilit:
- Position of the amino terminus of myosin light chain 1 and light chain 2 determined by electron microscopy with monoclonal antibodyJournal of Molecular Biology, 1987
- The amino acid sequence of ascidian (Halocynthia roretzi) myosin light chainsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- Complete nucleotide and encoded amino acid sequence of a mammalian myosin heavy chain geneJournal of Molecular Biology, 1986
- Location of the SH group of the alkali light chain on the myosin head as revealed by electron microscopyJournal of Molecular Biology, 1985
- Prediction of chain flexibility in proteinsThe Science of Nature, 1985
- Prediction of a triple-stranded coiled-coil region in tropomyosin-troponin T complexJournal of Theoretical Biology, 1982
- The role of myosin light chains in regulating actin-myosin interactionBiochimie, 1981
- Identification of the divalent metal ion binding domain of myosin regulatory light chains using spin-labelling techniquesJournal of Molecular Biology, 1980
- Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteinsJournal of Molecular Biology, 1978
- Analysis of the primary structure of collagen for the origins of molecular packingJournal of Molecular Biology, 1973