The reactive SH1 and SH2 cysteines in myosin subfragment 1 are cross-linked at similar rates with reagents of different length
- 1 May 1982
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 106 (1) , 117-122
- https://doi.org/10.1016/0006-291x(82)92066-6
Abstract
No abstract availableThis publication has 16 references indexed in Scilit:
- Proton Nuclear‐Magnetic‐Resonance Spectroscopy of Myosin Subfragment 1 IsoenzymesEuropean Journal of Biochemistry, 1981
- Reaction of 5,5'-dithiobis(2-nitrobenzoic acid) with myosin subfragment one: evidence for formation of a single protein disulfide with trapping of metal nucleotide at the active siteBiochemistry, 1980
- On the question of co-operative interaction of myosin heads with F-actin in the presence of ATPJournal of Molecular Biology, 1980
- Internal motions in myosinBiochemistry, 1979
- p-NN′-phenylenebismaleimide, a specific cross-linking agent for F-actinBiochemical Journal, 1978
- Effect of nucleotide binding on the proximity of the essential sulfhydryl groups of myosin. Chemical probing of movement of residues during conformational transitionsBiochemistry, 1977
- Reactivity of essential thiols of myosin. Chemical probes of the activated stateBiochemistry, 1977
- Spatial proximity of the two essential sulfhydryl groups of myosinBiochemistry, 1974