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Regulatory light‐chain Cys‐55 sites on the two heads of myosin can come within 2Å of each other
Author(s) -
Bower Susanne M.,
Wang Yulai,
Chantler Peter D.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81313-b
Subject(s) - myosin , immunoglobulin light chain , chemistry , chain (unit) , biophysics , myosin light chain kinase , biochemistry , microbiology and biotechnology , biology , genetics , physics , antibody , astronomy
The di‐thiol reagent, 5,5′‐dithiobis (2‐nitrobenzoic acid) is shown to induce disulfide bond formation between Mercenaria regulatory light‐chain Cys‐55 sites on either head of scallop hybrid myosin. This indicates that these two sites on opposite heads of myosin can come within 2Å of each other and this confirms a prediction based on earlier data [Chantler, Tao and Stafford (1991) Biophys. J. 59, 1242–1250]. Results demonstrate that myosin heads in solution show a considerable mutual freedom of movement which can be monitored by probes in the vicinity of regulatory light‐chain residue 55. Implications for light‐chain movement on the myosin head are discussed.