How sequence determines elasticity of disordered proteins

• Verfasst von: Cheng, Shanmei [VerfasserIn]
• Verfasst von: Cetinkaya, Murat [VerfasserIn]
• Verfasst von: Gräter, Frauke [VerfasserIn]
• Titel: How sequence determines elasticity of disordered proteins
• Verf.angabe: Shanmei Cheng, Murat Cetinkaya, and Frauke Gräter
• E-Jahr: 2010
• Jahr: 14 December 2010
• Umfang: 7 S.
• Fussnoten: Gesehen am 07.03.2023
• Titel Quelle: Enthalten in: Biophysical journal
• Ort Quelle: Cambridge, Mass. : Cell Press, 1960
• Jahr Quelle: 2010
• Band/Heft Quelle: 99(2010), 12, Seite 3863-3869
• ISSN Quelle: 1542-0086
• DOI: doi:10.1016/j.bpj.2010.10.011
• Datenträger: Online-Ressource
• Sprache: eng
• K10plus-PPN: 1838479457

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.