Pincus blob elasticity in an intrinsically disordered protein
- PMID: 37847354
- DOI: 10.1140/epje/s10189-023-00360-0
Pincus blob elasticity in an intrinsically disordered protein
Erratum in
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Correction to: Pincus blob elasticity in an intrinsically disordered protein.Eur Phys J E Soft Matter. 2023 Dec 8;46(12):125. doi: 10.1140/epje/s10189-023-00382-8. Eur Phys J E Soft Matter. 2023. PMID: 38063974 No abstract available.
Abstract
Understanding the dynamic structure of intrinsically disordered proteins (IDPs) is important to deciphering their biological functions. Here, we exploit precision entropic elasticity measurements to infer the conformational behavior of a model IDP construct formed from the disordered tail of the neurofilament low molecular weight protein. The IDP construct notably displays a low-force power-law elastic regime, consistent with the Pincus blob model, which allows direct extraction of the Flory exponent, [Formula: see text], from the force-extension relationship. We find [Formula: see text] increases with added denaturant, transitioning from a nearly ideal chain to a swollen chain in a manner quantitatively consistent with measurements of IDP dimensions from other experimental techniques. We suggest that measurements of entropic elasticity could be broadly useful in the study of IDP structure.
© 2023. The Author(s), under exclusive licence to EDP Sciences, SIF and Springer-Verlag GmbH Germany, part of Springer Nature.
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