| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Center for Biophysical Modeling and Simulation and Department of Chemistry, University of Utah, Salt Lake City, Utah
Correspondence: Address reprint requests to G. A. Voth, Tel.: 801-581-7272; E-mail: voth{at}chem.utah.edu.
Nonequilibrium molecular dynamics simulations were used to calculate the elastic properties of a spectrin repeat unit. A contiguous
-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.
This article has been cited by other articles:
![]() |
L. G. Randles, R. W. S. Rounsevell, and J. Clarke Spectrin Domains Lose Cooperativity in Forced Unfolding Biophys. J., January 15, 2007; 92(2): 571 - 577. [Abstract] [Full Text] [PDF] |
||||
![]() |
S. Paramore and G. A. Voth Examining the Influence of Linkers and Tertiary Structure in the Forced Unfolding of Multiple-Repeat Spectrin Molecules Biophys. J., November 1, 2006; 91(9): 3436 - 3445. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |