Invited review: probing the structures of muscle regulatory proteins using small-angle solution scattering

dc.contributor.authorLu, YLen_AU
dc.contributor.authorJeffries, CMen_AU
dc.contributor.authorTrewhella, Jen_AU
dc.date.accessioned2012-02-09T01:44:40Zen_AU
dc.date.available2012-02-09T01:44:40Zen_AU
dc.date.issued2011-08-01en_AU
dc.date.statistics2012-01-09en_AU
dc.description.abstractSmall-angle X-ray and neutron scattering with contrast variation have made important contributions in advancing our understanding of muscle regulatory protein structures in the context of the dynamic molecular processes governing muscle action. The contributions of the scattering investigations have depended upon the results of key crystallographic, NMR, and electron microscopy experiments that have provided detailed structural information that has aided in the interpretation of the scattering data. This review will cover the advances made using small-angle scattering techniques, in combination with the results from these complementary techniques, in probing the structures of troponin and myosin binding protein C. A focus of the troponin work has been to understand the isoform differences between the skeletal and cardiac isoforms of this major calcium receptor in muscle. In the case of myosin binding protein C, significant data are accumulating, indicating that this protein may act to modulate the primary calcium signals from troponin, and interest in its biological role has grown because of linkages between gene mutations in the cardiac isoform and serious heart disease. (C) 2011 Wiley Periodicals, Inc. Biopolymers 95: 505-516, 2011.en_AU
dc.identifier.citationLu, Y.L., Jeffries, C.M., Trewhella, J. (2011). Invited review: probing the structures of muscle regulatory proteins using small-angle solution scattering. Biopolymers, 95(8, SI), 505-516. doi:doi:10.1002/bip.21624en_AU
dc.identifier.govdoc3869en_AU
dc.identifier.issn0006-3525en_AU
dc.identifier.issue8, SIen_AU
dc.identifier.journaltitleBiopolymersen_AU
dc.identifier.pagination505-516en_AU
dc.identifier.urihttp://dx.doi.org/10.1002/bip.21624en_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/3999en_AU
dc.identifier.volume95en_AU
dc.language.isoenen_AU
dc.publisherWiley-Blackwellen_AU
dc.subjectSmall angle scatteringen_AU
dc.subjectCrystal structureen_AU
dc.subjectX-ray diffractionen_AU
dc.subjectNeutron diffractionen_AU
dc.subjectMusclesen_AU
dc.subjectProteinsen_AU
dc.titleInvited review: probing the structures of muscle regulatory proteins using small-angle solution scatteringen_AU
dc.typeJournal Articleen_AU
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