Toward Protein Structure In Situ: Comparison of Two Bifunctional Rhodamine Adducts of Troponin C

This publication has 24 references indexed in Scilit:

• Structural changes in troponin in response to Ca ²⁺ and myosin binding to thin filaments during activation of skeletal muscle
  Proceedings of the National Academy of Sciences, 2006
• Photomodulation of ionic current through hemithioindigo-modified gramicidin channels
  Organic & Biomolecular Chemistry, 2004
• Configuration of the two kinesin motor domains during ATP hydrolysis
  Nature Structural & Molecular Biology, 2003
• Myosin V Walks Hand-Over-Hand: Single Fluorophore Imaging with 1.5-nm Localization
  Science, 2003
• In Situ Orientations of Protein Domains: Troponin C in Skeletal Muscle Fibers
  Molecular Cell, 2003
• NMR Structure of a Bifunctional Rhodamine Labeled N-Domain of Troponin C Complexed with the Regulatory “Switch” Peptide from Troponin I: Implications for in Situ Fluorescence Studies in Muscle Fibers^,
  Biochemistry, 2003
• Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization
  Nature, 2003
• Optical Switching of Ion−Dipole Interactions in a Gramicidin Channel Analogue
  Journal of the American Chemical Society, 2000
• A Homobifunctional Rhodamine for Labeling Proteins with Defined Orientations of a Fluorophore
  Bioconjugate Chemistry, 1998
• NMRPipe: A multidimensional spectral processing system based on UNIX pipes
  Journal of Biomolecular NMR, 1995