Spectroscopic probes of muscle proteins

D. D. Thomas, J. M. Muretta, B. A. Colson, R. N. Mello, D. Kast

Research output: Chapter in Book/Report/Conference proceedingChapter

11 Scopus citations

Abstract

The use of site-directed spectroscopic probes in elucidating the molecular mechanism of force generation in muscle is reviewed, focusing on recent technical and conceptual advances. High-resolution crystal structures of actin and myosin suggest mechanistic models for force generation, but spectroscopic probe experiments under functional conditions are required to test and refine these models. An array of complementary spectroscopic techniques has been developed that can detect disorder and dynamics directly, resolve multiple conformational states, and can be applied to complex protein assemblies, taking advantage of the beautiful symmetry of the myofibrillar lattice. Recently developed instrumentation has the capacity to resolve simultaneously both biochemical and structural kinetics of myosin and/or actin. These new insights support a model in which structural and biochemical transitions are not tightly coupled, and disorder-to-order transitions play central roles in both force generation and its regulation.

Original languageEnglish
Title of host publicationComprehensive Biophysics
PublisherElsevier Inc.
Pages226-250
Number of pages25
Volume4
ISBN (Print)9780080957180
DOIs
StatePublished - Dec 1 2012
Externally publishedYes

Keywords

  • Actin
  • DEER
  • Disorder
  • Dynamics
  • EPR
  • FRET
  • Fluorescence
  • Force generation
  • Myosin
  • Spin label
  • Structural kinetics
  • TPA
  • Time-resolved

Fingerprint Dive into the research topics of 'Spectroscopic probes of muscle proteins'. Together they form a unique fingerprint.

  • Cite this

    Thomas, D. D., Muretta, J. M., Colson, B. A., Mello, R. N., & Kast, D. (2012). Spectroscopic probes of muscle proteins. In Comprehensive Biophysics (Vol. 4, pp. 226-250). Elsevier Inc.. https://doi.org/10.1016/B978-0-12-374920-8.00415-X