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pubmed-article:10962092pubmed:abstractTextStructural changes in subfragment 1 of skeletal muscle myosin were investigated by cross-linking trypsin-cleaved S1 with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide. In the absence of nucleotide the alkali light chains are cross-linked to the 27 kDa heavy chain fragment; the presence of MgATP reduces the efficiency of this reaction. On the other hand, MgATP promotes the cross-link formation between the N-terminal 27 kDa and C-terminal 20 kDa fragments of the heavy chain. The chemical cleavage of the cross-linked heavy chains fragments with N-chlorosuccinimide and hydroxylamine indicates that the cross-links are formed between the regions spanning residues 131-204 and 699-809. These results indicate that the two regions of the heavy chain that are relatively distant in nucleotide-free skeletal S1 [Rayment et al. (1993) Science 261, 50-58] can potentially interact upon addition of nucleotide.lld:pubmed
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pubmed-article:10962092pubmed:dateRevised2009-11-19lld:pubmed
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pubmed-article:10962092pubmed:articleTitleNucleotide-induced movements in the myosin head near the converter region.lld:pubmed
pubmed-article:10962092pubmed:affiliationDepartment of Muscle Biochemistry, Nencki Institute of Experimental Biology, 3 Pasteur St., PL-02-093 Warsaw, Poland. basiap@nencki.gov.pllld:pubmed
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pubmed-article:10962092pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed