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Compressibility and specific volume of actin decrease upon G to F transformation

N Suzuki1, Y Tamura, K Mihashi

  • 1Department of Physics, School of Science, Nagoya University, Japan.

Biochimica Et Biophysica Acta
|February 8, 1996
PubMed
Summary
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Globular actin (G-actin) is soft, while filamentous actin (F-actin) shows increased hydration upon polymerization. Calcium binding to thin filaments affects inter-subunit junctions, not the actin subunit itself.

Area of Science:

  • Biophysics
  • Protein Biochemistry
  • Muscle Physiology

Background:

  • Actin polymerization is fundamental to muscle contraction and cellular dynamics.
  • Understanding actin's structural and dynamic properties is crucial for elucidating its functions.
  • Calcium ions play a key role in regulating muscle function via the thin filament.

Purpose of the Study:

  • To investigate the volume and compressibility changes of actin during polymerization.
  • To detect conformational changes in the reconstituted thin filament upon Ca2+ binding.
  • To characterize the biophysical properties of G-actin, F-actin, and the reconstituted thin filament.

Main Methods:

  • Measurement of solution densities and sound velocities.
  • Determination of partial specific volumes and partial specific adiabatic compressibilities.

Related Experiment Videos

  • Analysis of G-actin, F-actin, and reconstituted thin filament under varying conditions.

    • Main Results:

    • G-actin exhibits a high partial specific adiabatic compressibility (9.3 x 10^-12 cm2/dyne), suggesting it is a soft protein.
    • F-actin shows significantly lower partial specific volumes (0.63-0.66 cm3/g) and negative compressibilities (-(7-13) x 10^-12 cm2/dyne), indicating increased hydration upon polymerization.
    • Little difference in compressibility was observed between Ca2+-bound and Ca2+-unbound states of the reconstituted thin filament.

    Conclusions:

    • Actin polymerization involves substantial changes in volume and hydration, with F-actin being less compressible than G-actin.
    • The negative compressibility of F-actin suggests a significant increase in bound water molecules.
    • Ca2+ binding to the thin filament primarily influences inter-subunit interactions rather than altering the actin subunit's conformation.