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

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

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 conference › Paper › peer-review

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 et al. [R. Ivkov, J. G. Forbes, and S. C. Greer, J. Chem. Phys. 108, 5599 (1998)], were taken in D2O 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 (of O. Glatter and coworkers) provides 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 the G-actin monomer, under the conditions given above, is a sphere 50-54 angstroms 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 language	English (US)
Number of pages	1
State	Published - Dec 1 2005
Externally published	Yes
Event	05AIChE: 2005 AIChE Annual Meeting and Fall Showcase - Cincinnati, OH, United States Duration: Oct 30 2005 → Nov 4 2005

Other

Other	05AIChE: 2005 AIChE Annual Meeting and Fall Showcase
Country/Territory	United States
City	Cincinnati, OH
Period	10/30/05 → 11/4/05

ASJC Scopus subject areas

General Engineering

Cite this

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title = "The polymerization of actin: Structural changes from small angle neutron scattering",

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 et al. [R. Ivkov, J. G. Forbes, and S. C. Greer, J. Chem. Phys. 108, 5599 (1998)], were taken in D2O 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 (of O. Glatter and coworkers) provides 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 the G-actin monomer, under the conditions given above, is a sphere 50-54 angstroms 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.",

author = "Norman, {Alexander I.} and Robert Ivkov and Forbes, {Jeffrey G.} and Greer, {Sandra C.}",

year = "2005",

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note = "05AIChE: 2005 AIChE Annual Meeting and Fall Showcase ; Conference date: 30-10-2005 Through 04-11-2005",

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T1 - The polymerization of actin

T2 - 05AIChE: 2005 AIChE Annual Meeting and Fall Showcase

AU - Norman, Alexander I.

AU - Ivkov, Robert

AU - Forbes, Jeffrey G.

AU - Greer, Sandra C.

PY - 2005/12/1

Y1 - 2005/12/1

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 et al. [R. Ivkov, J. G. Forbes, and S. C. Greer, J. Chem. Phys. 108, 5599 (1998)], were taken in D2O 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 (of O. Glatter and coworkers) provides 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 the G-actin monomer, under the conditions given above, is a sphere 50-54 angstroms 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 et al. [R. Ivkov, J. G. Forbes, and S. C. Greer, J. Chem. Phys. 108, 5599 (1998)], were taken in D2O 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 (of O. Glatter and coworkers) provides 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 the G-actin monomer, under the conditions given above, is a sphere 50-54 angstroms 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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Y2 - 30 October 2005 through 4 November 2005

ER -

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

Abstract

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