ArticleBiophysical journal2007
Toward protein structure in situ: comparison of two bifunctional rhodamine adducts of troponin C.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- Development of bifunctional fluorescent probes and their application to α-helix labelling.Organic & biomolecular chemistry · 2025Article
- Structural changes in troponin during activation of skeletal and heart muscle determined in situ by polarised fluorescence.Biophysical reviews · 2024Review
- Stress-dependent activation of myosin in the heart requires thin filament activation and thick filament mechanosensing.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Single molecule optical measurements of orientation and rotations of biological macromolecules.Methods and applications in fluorescence · 2016Article
- Orientation of the N- and C-terminal lobes of the myosin regulatory light chain in cardiac muscle.Biophysical journal · 2015Article
- Orientation of the N-terminal lobe of the myosin regulatory light chain in skeletal muscle fibers.Biophysical journal · 2012Article
- Structure and dynamics of the kinesin-microtubule interaction revealed by fluorescence polarization microscopy.Methods in cell biology · 2010Review
- Calcium- and myosin-dependent changes in troponin structure during activation of heart muscle.The Journal of physiology · 2009Article
- Orientation of the essential light chain region of myosin in relaxed, active, and rigor muscle.Biophysical journal · 2008Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
As part of a program to develop methods for determining protein structure in situ, sTnC was labeled with a bifunctional rhodamine (BR or BSR), cross-linking residues 56 and 63 of its C-helix. NMR spectroscopy of the N-terminal domain of BSR-labeled sTnC in complex with Ca(2+) and the troponin I switch peptide (residues 115-131) showed that BSR labeling does not significantly affect the secondary structure of the protein or its dynamics in solution. BR-labeling was previously shown to have no effect on the solution structure of this complex. Isometric force generation in isolated demembranated fibers from rabbit psoas muscle into which BR- or BSR-labeled sTnC had been exchanged showed reduced Ca(2+)-sensitivity, and this effect was larger with the BSR label. The orientation of rhodamine dipoles with respect to the fiber axis was determined by polarized fluorescence. The mean orientations of the BR and BSR dipoles were almost identical in relaxed muscle, suggesting that both probes accurately report the orientation of the C-helix to which they are attached. The BSR dipole had smaller orientational dispersion, consistent with less flexible linkers between the rhodamine dipole and cysteine-reactive groups.
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Registered trials
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