The polymerization of actin: Structural changes from small-angle neutron scattering

Alexander I. Norman, Robert Ivkov, Jeffrey G. Forbes, Sandra C. Greer

Research output: Contribution to journalArticle

Abstract

We present a new analysis of small-angle neutron-scattering data from rabbit muscle actin in the course of the polymerization from G -actin to F -actin as a function of temperature. The data, from Ivkov [J. Chem. Phys. 108, 5599 (1998)], were taken in D2 O buffer with Ca2+ as the divalent cation on the G -actin in the presence of ATP and with KCl as the initiating salt. The new analysis of the data using modeling and the method of generalized indirect fourier transform (O. Glatter, GIFT, University of Graz, Austria, http://physchem.kfunigraz.ac.at/sm/) provide shapes and dimensions of the G -actin monomer and of the growing actin oligomer in solution as a function of temperature and salt concentration. This analysis indicates that the G -actin monomer, under the conditions given above, is a sphere 50-54 Å in diameter as opposed to the oblate ellipsoid seen by x-ray crystallography. The F -actin dimensions are consistent with x-ray crystal structure determinations.

Original languageEnglish (US)
Article number154904
JournalJournal of Chemical Physics
Volume123
Issue number15
DOIs
StatePublished - Oct 15 2005
Externally publishedYes

ASJC Scopus subject areas

  • Physics and Astronomy(all)
  • Physical and Theoretical Chemistry

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