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dc.contributor.authorLing, Nicholas
dc.contributor.authorShrimpton, C.
dc.contributor.authorSleep, J.
dc.contributor.authorKendrick-Jones, J.
dc.contributor.authorIrving, M.
dc.coverage.spatialUNITED STATESen_NZ
dc.date.accessioned2008-11-07T00:59:20Z
dc.date.available2008-11-07T00:59:20Z
dc.date.issued1996-04
dc.identifier.citationLing, N., Shrimpton, C., Sleep, J., Kendrick-Jones, J. & Irving, M. (1996). Fluorescent probes of the orientation of myosin regulatory light chains in relaxed, rigor, and contracting muscle. Biophysical Journal, 70, 1836- 1846.en_US
dc.identifier.issn1542-0086
dc.identifier.urihttps://hdl.handle.net/10289/1290
dc.description.abstractThe orientation of the light-chain region of myosin heads in relaxed, rigor, and isometrically contracting fibers from rabbit psoas muscle was studied by fluorescence polarization. Cysteine 108 of chicken gizzard myosin regulatory light chain (cgRLC) was covalently modified with iodoacetamidotetramethylrhodamine (iodo-ATR). Native RLC of single glycerinated muscle fibers was exchanged for labeled cgRLC in a low [Mg2+] rigor solution at 30 degrees C. Troponin and troponin C removed in this procedure were replaced. RLC exchange had little effect on active force production. X-ray diffraction showed normal structure in rigor after RLC exchange, but loss of axial and helical order in relaxation. In isolated myofibrils labeled cgRLC was confined to the regions of the sarcomere containing myosin heads. The ATR dipoles showed a preference for orientations perpendicular to the fiber axis, combined with limited nanosecond rotational motion, in all conditions studied. The perpendicular orientation preference was more marked in rigor than in either relaxation or active contraction. Stretching relaxed fibers to sarcomere length 4 microns to eliminate overlap between actin- and myosin-containing filaments had little effect on the orientation preference. There was no change in orientation preference when fibers were put into rigor at sarcomere length 4.0 microns. Qualitatively similar results were obtained with ATR-labeled rabbit skeletal RLC.en_US
dc.format.mimetypeapplication/pdf
dc.language.isoen
dc.publisherBiophysical Societyen_NZ
dc.relation.urihttp://www.biophysj.org/cgi/content/abstract/70/4/1836en_US
dc.rightsThis article has been published in the journal: Biophysical Journal. Copyright © 1996 by the Biophysical Society.en_US
dc.titleFluorescent probes of the orientation of myosin regulatory light chains in relaxed, rigor, and contracting muscle.en_US
dc.typeJournal Articleen_US
dc.identifier.doi10.1016/S0006-3495(96)79749-7en_NZ
dc.relation.isPartOfBiophysical Journalen_NZ
pubs.begin-page1836en_NZ
pubs.elements-id33625
pubs.end-page1846en_NZ
pubs.issue4en_NZ
pubs.volume70en_NZ


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