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Extending a Spectrin Repeat Unit. I: Linear Force-extension Response

Overview
Journal Biophys J
Publisher Cell Press
Specialty Biophysics
Date 2005 Oct 18
PMID 16227506
Citations 12
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Abstract

Nonequilibrium molecular dynamics simulations were used to calculate the elastic properties of a spectrin repeat unit. A contiguous alpha-helical linker was constructed by employing periodic boundary conditions, allowing a novel scheme for evaluating the thermodynamic force as a function of extension. By measuring the force-extension response under small extensions, spectrin was observed to behave primarily as an elastic material with a spring constant of 1700 +/- 100 pN/nm. The implications of this spring constant, in terms of the properties of the spectrin tetramer, are also discussed.

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References
1.
Speicher D, DeSilva T, Speicher K, Ursitti J, Hembach P, Weglarz L . Location of the human red cell spectrin tetramer binding site and detection of a related "closed" hairpin loop dimer using proteolytic footprinting. J Biol Chem. 1993; 268(6):4227-35. View

2.
SHOTTON D, Burke B, Branton D . The molecular structure of human erythrocyte spectrin. Biophysical and electron microscopic studies. J Mol Biol. 1979; 131(2):303-29. DOI: 10.1016/0022-2836(79)90078-0. View

3.
Yan Y, Winograd E, Viel A, Cronin T, Harrison S, Branton D . Crystal structure of the repetitive segments of spectrin. Science. 1993; 262(5142):2027-30. DOI: 10.1126/science.8266097. View

4.
Lu H, Schulten K . The key event in force-induced unfolding of Titin's immunoglobulin domains. Biophys J. 2000; 79(1):51-65. PMC: 1300915. DOI: 10.1016/S0006-3495(00)76273-4. View

5.
Speicher D, Marchesi V . Erythrocyte spectrin is comprised of many homologous triple helical segments. Nature. 1984; 311(5982):177-80. DOI: 10.1038/311177a0. View