ArticleBiophysical journal2010
How sequence determines elasticity of disordered proteins.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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28 citing papers in PubMed, 73 citations in OpenAlex.
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- On the nuclear pore complex and its emerging role in cellular mechanotransduction.APL bioengineering · 2022Review
- Full structural ensembles of intrinsically disordered proteins from unbiased molecular dynamics simulations.Communications biology · 2021Article
- The structural basis of Rubisco phase separation in the pyrenoid.Nature plants · 2020Article
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- Architectural Dynamics of CaMKII-Actin Networks.Biophysical journal · 2019Article
- Squid-Inspired Tandem Repeat Proteins: Functional Fibers and Films.Frontiers in chemistry · 2019Review
- The impact ofChemical science · 2018Article
- The Eukaryotic COCell · 2017Article
- Proteus: a random forest classifier to predict disorder-to-order transitioning binding regions in intrinsically disordered proteins.Journal of computer-aided molecular design · 2017Article
- Proteomic analysis reveals diverse proline hydroxylation-mediated oxygen-sensing cellular pathways in cancer cells.Oncotarget · 2016Article
- Can Dissipative Properties of Single Molecules Be Extracted from a Force Spectroscopy Experiment?Biophysical journal · 2016Article
- Optimal numbers of residues in linkers of DNA polymerase I, T7 primase and DNA polymerase IV.Scientific reports · 2016Article
- The Widespread Prevalence and Functional Significance of Silk-Like Structural Proteins in Metazoan Biological Materials.PloS one · 2016Article
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Authors and funding
3 authors at 1 institution in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
How nature tunes sequences of disordered protein to yield the desired coiling properties is not yet well understood. To shed light on the relationship between protein sequence and elasticity, we here investigate four different natural disordered proteins with elastomeric function, namely: FG repeats in the nucleoporins; resilin in the wing tendon of dragonfly; PPAK in the muscle protein titin; and spider silk. We obtain force-extension curves for these proteins from extensive explicit solvent molecular dynamics simulations, which we compare to purely entropic coiling by modeling the four proteins as entropic chains. Although proline and glycine content are in general indicators for the entropic elasticity as expected, divergence from simple additivity is observed. Namely, coiling propensities correlate with polyproline II content more strongly than with proline content, and given a preponderance of glycines for sufficient backbone flexibility, nonlocal interactions such as electrostatic forces can result in strongly enhanced coiling, which results for the case of resilin in a distinct hump in the force-extension curve. Our results, which are directly testable by force spectroscopy experiments, shed light on how evolution has designed unfolded elastomeric proteins for different functions.
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