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- W314850954 abstract "A hydrodynamic, enzymatic and CD spectroscopic study of skeletal muscle myosin light chain kinase, three proteolytic fragments and corresponding complexes with calmodulin was performed. A refined shape model was built for the enzyme. It was shown that a head-and-tail structure is formed from two major fragments which are aligned end-to-end. The one fragment (Mr 36000) is compact, of high alpha-helix content and contains the catalytic center with the light chain and the calmodulin binding domains. The other fragment (Mr 33000) with unknown function is asymmetric (a/b greater than 10), of low alpha-helix and of unusually high proline content." @default.
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- W314850954 date "1983-07-04" @default.
- W314850954 modified "2023-09-26" @default.
- W314850954 title "Skeletal muscle myosin light chain kinase" @default.
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- W314850954 doi "https://doi.org/10.1016/0014-5793(83)80552-3" @default.
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