TY - JOUR
T1 - The polymerization of actin
T2 - Structural changes from small-angle neutron scattering
AU - Norman, Alexander I.
AU - Ivkov, Robert
AU - Forbes, Jeffrey G.
AU - Greer, Sandra C.
N1 - Funding Information:
This research was supported by the National Science Foundation, Chemistry Division. The authors acknowledge the support of the National Institute of Standards and Technology, U. S. Department of Commerce in providing the neutron research facilities used in this work. One of the authors (J.F.) thanks Kuan Wang, Chief of LMB, NIAMS for the encouragement and support of this project. Another author (S.G.) acknowledges the support of the University of Maryland College Park, Division of Research and Graduate Studies.
PY - 2005/10/15
Y1 - 2005/10/15
N2 - 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.
AB - 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.
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U2 - 10.1063/1.2039088
DO - 10.1063/1.2039088
M3 - Article
C2 - 16252969
AN - SCOPUS:28344442377
SN - 0021-9606
VL - 123
JO - Journal of Chemical Physics
JF - Journal of Chemical Physics
IS - 15
M1 - 154904
ER -