Crosslinked myosin subfragment 1: a stable analogue of the subfragment-1.ATP complex.
نویسندگان
چکیده
منابع مشابه
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...
متن کاملSubfragment 1 of cow carotid myosin.
This enzymatically active subunit of smooth muscle myosin has not so far been isolated. Previous work on cow carotid myosin [l] and on chicken gizzard myosin [2] has revealed that these myosins are, as cardiac myosin [3, cf. 4] much more resistant to tryptic digestion than rabbit skeletal myosin. Furthermore, if the L-meromyosin (LMM) obtained behaves on the whole similarly to its skeletal coun...
متن کاملProtease-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...
متن کاملThe interaction of chromophoric nucleotides with subfragment 1 of myosin.
The interaction of a series of chromophoric nucleotides derived from 6-mercapto-9-beta-ribofuranosylpurine (thioinosine, thiol) and 2-amino-6-mercapto-9-beta-ribofuranosyl-purine (thioguanosine, thioG) with myosin subfragment 1 isolated from rabbit skeletal muscle was investigated kinetically and spectroscopically. The Mg2+-dependent hydrolyses of thioITP and thioGTP are catalysed by subfragmen...
متن کاملBinding of myosin subfragment-1 to F-actin.
During a part of the hydrolytic cycle, myosin head (S1) carries no nucleotide and binds strongly to an actin filament forming a rigor bond. At saturating concentration of S1 in rigor, S1 is well known to form 1:1 complex with actin. However, we have provided evidence that under certain conditions S1 could also form a complex with 2 actin monomers in a filament (Andreev, O.A. & Borejdo, J. (1991...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1983
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.80.16.4909