Stabilization of a primary loop in myosin subfragment 1 with a fluorescent crosslinker.

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Stabilization of a primary loop in myosin subfragment 1 with a fluorescent crosslinker.

A bifunctional fluorescent alkylating agent, dibromobimane, has been used to stabilize a preexisting primary loop in myosin subfragment 1 (S-1). The crosslink achieved joins Cys-707 (called sulfhydryl group "SH1") of the 20-kDa domain (formerly called "20K" domain) with a thiol of the 50-kDa domain and seems to place the dibromobimane near the ATP-perturbable tryptophan.

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The interdomain motions in myosin subfragment 1.

The interdomain motions in myosin subfragment 1 (S1) were studied by steady-state and time-resolved fluorescence of tryptophan residues and N-(iodoacetyl)-N'-(5-sulfo-1-naphtyl)ethylenediamine (AEDANS) attached to Cys178 of alkali light chain 1 (A1) exchanged into S1. The efficiency of fluorescence resonance energy transfer (FRET) from tryptophan residues of motor domain to AEDANS at A1 decreas...

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Protease-sensitive regions in myosin subfragment 1.

Proteolytic digestions of myosin subfragment 1 (S-1) with elastase, subtilisin, papain, thermolysin, and Staphylococcus aureus protease reveal that the two trypsin-sensitive regions in S-1 have broad protease susceptibility. The cleavage of S-1 by these enzymes yields products that correspond within 1-2 kilodaltons (kDa) to the 25-, 50-, and 20-kDa fragments produced by trypsin. Papain and ther...

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Subfragment 1 of cow carotid myosin.

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 1985

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.82.6.1658