Vibrational Modes of G-Actin
The determination of the atomic structure of g-actin (Kabsch et al., 1990, see Fig. 1) allowed the development of an atomic model for f-actin (Holmes et al., 1990). The structure of f-actin was deduced from x-ray diffraction patterns from bundles of aligned actin filaments, using the known helical symmetry of the filament and keeping the atomic structure of the monomer fixed. The model of f-actin was obtained, therefore, using only four structural parameters: three rotational and one radial degree of freedom. The solution thus obtained is unique, and achieved an R-factor of.22; an extremely good fit with such few parameters.
KeywordsNormal Mode Slow Mode Normal Mode Analysis Binding Loop Hinge Point
Unable to display preview. Download preview PDF.
- Brooks, B & Karplus, B., 1983, Harmonic dynamics of proteins: Normal modes and fluctuations in bovine pancreatic trypsin inhibitor, Biophysics 80: 6571.Google Scholar
- Diamond, R., 1990, On the use of normal modes in thermal parameter refinement: theory and application to bovine pancreatic trypsin inhibitor, Acta Cryst. A46: 425.Google Scholar
- Goldstein, H., 1950, “Classical Mechanics”, Addison-Wesley, Reading, Massachusetts.Google Scholar
- Millonig, R., Siitterlin, R., Engel, A., Pollard, T. D., Aebi, U., 1989, The ‘lateral slipping’ model of F-actin filaments, in: “Springer Series In Biophysics Vol. 3, Cytoskeletal and Extracellular Proteins” U. Aebi and A. Engel, eds., Springer-Verlag, Heidelberg Google Scholar
- Orlova, A. and Egelman, E. H., 1993, A conformational change in the actin subunit can change the flexibility of the actin filament. J. Mol. Biol. In press.Google Scholar