ArticleProceedings of the National Academy of Sciences of the United States of America2008
Unique elastic properties of the spectrin tetramer as revealed by multiscale coarse-grained modeling.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 29 citations in OpenAlex.
- Structural Configuration of Blood Cell Membranes Determines Their Nonlinear Deformation Properties.BioMed research international · 2022Article
- Empirical and Computational Comparison of Alternative Therapeutic Exon Skip Repairs for Duchenne Muscular Dystrophy.Biochemistry · 2019Article
- Fine mapping of hydrophobic contacts reassesses the organization of the first three dystrophin coiled-coil repeats.Protein science : a publication of the Protein Society · 2019Article
- Rhombic organization of microvilli domains found in a cell model of the human intestine.PloS one · 2018Article
- The Physiological Molecular Shape of Spectrin: A Compact Supercoil Resembling a Chinese Finger Trap.PLoS computational biology · 2015Article
- Transformation of membrane nanosurface of red blood cells under hemin action.Scientific reports · 2014Article
- High ferritin levels have major effects on the morphology of erythrocytes in Alzheimer's disease.Frontiers in aging neuroscience · 2013Article
- Sequence composition and environment effects on residue fluctuations in protein structures.The Journal of chemical physics · 2010Article
- Systematic coarse-graining of spectrin-level red blood cell models.Computer methods in applied mechanics and engineering · 2010Article
- Molecular dynamics simulation and coarse-grained analysis of the Arp2/3 complex.Biophysical journal · 2008Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The force-extension profile of tetrameric spectrin is determined by using multiscale computer simulation. Fluctuation results of atomistic simulations of double spectrin repeat units (DSRU) are used to systematically build a coarse-grained (CG) model for the tetrameric form of spectrin. It is found that the spectrin tetramer can be modeled as a soft polymer with a unique flat force-extension profile over the range of biologically important lengths. It is also concluded that in the cytoskeletal network of the red blood cell the tetramer is in an "overcompressed" state. These findings are in contrast to the commonly used models of spectrin tetramer elasticity, namely the "entropic spring" polymer models. From these results, it is concluded that stable intact helical linker regions are needed to maintain the soft elasticity of the spectrin tetramer.
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