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PMID: 16227506 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Extending a spectrin repeat unit. I: linear force-extension response.

Biophysical journal ·Vol. 90 ·No. 1 ·2006-01-01 ·Pages 92-100

Paramore S, Ayton GS, Mirijanian DT, Voth GA

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.

MeSH Terms
Algorithms Animals Biophysics/methods Brain/metabolism Carbon/chemistry Chickens Computer Simulation Cytoskeleton/chemistry Magnetic Resonance Spectroscopy Microscopy, Atomic Force/methods Models, Biological Models, Statistical Molecular Conformation Protein Conformation Protein Denaturation Protein Folding Protein Structure, Secondary Software Spectrin/chemistry,metabolism Thermodynamics Water/chemistry
Chemicals
Water Spectrin Carbon
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Paramore Sterling
Center for Biophysical Modeling and Simulation and Department of Chemistry, University of Utah, Salt Lake City, Utah, USA.
Ayton Gary S
Mirijanian Dina T
Voth Gregory A
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Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
DOI
10.1529/biophysj.105.066969
Published
2006-01-01
Epub
2005-00-14
Pages
92-100
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1367040
Subset
IM
External Links
PubMed source DOI: 10.1529/biophysj.105.066969 PMC Full Text View journal details
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