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 thi...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1985-03, Vol.82 (6), p.1658-1662
Main Authors: Mornet, Dominique, Ue, Kathleen, Morales, Manuel F.
Format: Article
Language:English
Subjects:
Actins
Adenosine triphosphatases
Analytical, structural and metabolic biochemistry
Animals
Biochemistry
Biological and medical sciences
Bridged Bicyclo Compounds
Contractile proteins
cross-linking
Cross-Linking Reagents
Crosslinking
Dyes
Fluorescence
Fluorescent Dyes
fluorescent probes
Fundamental and applied biological sciences. Psychology
Gels
Holoproteins
myosin
Myosin Subfragments
Myosins
Peptide Fragments
Protein Conformation
Proteins
Rabbits
Reagents
skeletal muscle
Sulfhydryl Compounds
Teeth
Thiols
Tryptophan
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Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.82.6.1658