The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Charge interactions can dominate the dimensions of intrinsically disordered proteins
Open accessAbstract
Many eukaryotic proteins are disordered under physiological conditions, and fold into ordered structures only on binding to their cellular targets. Such intrinsically disordered proteins (IDPs) often contain a large fraction of charged amino acids. Here, we use single-molecule Förster resonance energy transfer to investigate the influence of charged residues on the dimensions of unfolded and intrinsically disordered proteins. We find that, in contrast to the compact unfolded conformations that have been observed for many proteins at low denaturant concentration, IDPs can exhibit a prominent expansion at low ionic strength that correlates with their net charge. Charge-balanced polypeptides, however, can exhibit an additional collapse at low ionic strength, as predicted by polyampholyte theory from the attraction between opposite charges in the chain. The pronounced effect of charges on the dimensions of unfolded proteins has important implications for the cellular functions of IDPs.
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Citations
Cites
Intrinsically unstructured proteins and their functions
Dyson, H. J., & Wright, P. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1589 · Cited by 3,871
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Extreme disorder in an ultrahigh-affinity protein complex
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Self-citationTemperature-dependent solvation modulates the dimensions of disordered proteins
Wuttke, R., Hofmann, H., Nettels, D., Borgia, M. B., Mittal, J., Best, R. B., & Schuler, B. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1313006111 · Cited by 192
Self-citationInteractions by disorder – A matter of context
Bugge, K., Brakti, I., Fernandes, C. B., Dreier, J. E., Lundsgaard, J. E., Olsen, J. G., Skriver, K., & Kragelund, B. B. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.00110 · Cited by 155
“These altogether point toward compositional parameters such as the net charge (Marsh and Formankay, 2010; Muller-Spath et al., 2010) or more specifically the distribution of charges (Das and Pappu, 2013), and proline residues (Marsh and Forman-kay, 2010; Martin et al., 2016) as being key…”
BackgroundIdentification of an Aggregation-Prone Structure of Tau
Elbaum-Garfinkle, S., & Rhoades, E. (2012) · Journal of the American Chemical Society · doi:10.1021/ja305206m · Cited by 149
Describing sequence–ensemble relationships for intrinsically disordered proteins
Mao, A. H., Lyle, N., & Pappu, R. V. (2013) · Biochemical Journal · doi:10.1042/bj20121346 · Cited by 135
Conformational buffering underlies functional selection in intrinsically disordered protein regions
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A quantitative measure for protein conformational heterogeneity
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Sequence-to-conformation relationships of disordered regions tethered to folded domains of proteins
Mittal, A., Holehouse, A. S., Cohan, M. C., & Pappu, R. V. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.05.012 · Cited by 72
Quantifying the topography of the intrinsic energy landscape of flexible biomolecular recognition
Chu, X., Gan, L., Wang, E., & Wang, J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1220699110 · Cited by 62
Apolipoprotein E4 has extensive conformational heterogeneity in lipid-free and lipid-bound forms
Stuchell-Brereton, M. D., Zimmerman, M. I., Miller, J. J., Mallimadugula, U. L., Incicco, J. J., Roy, D., Smith, L. G., Cubuk, J., Baban, B., DeKoster, G. T., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2215371120 · Cited by 48
Self-citationWaszkiewicz, R., Michaś, A., Białobrzewski, M. K., Klepka, B. P., Cieplak-Rotowska, M. K., Staszałek, Z., Cichocki, B., Lisicki, M., Szymczak, P., & Niedzwiecka, A. (2024) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.4c00312 · Cited by 16
Metadata
- Authors
- Müller-Späth, S., Soranno, A., Hirschfeld, V., Hofmann, H., Rüegger, S., Reymond, L., Nettels, D., & Schuler, B.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2010-07-16
- Volume
- 107
- Issue
- 33
- Pages
- 14609-14614
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W3030183899
- Cited by
- 502
- References
- 1
- FWCI
- 10.87
- Type
- journal article
- Language
- en
- Open access
- green
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