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Relating sequence encoded information to form and function of intrinsically disordered proteins
Open accessAbstract
Intrinsically disordered proteins (IDPs) showcase the importance of conformational plasticity and heterogeneity in protein function. We summarize recent advances that connect information encoded in IDP sequences to their conformational properties and functions. We focus on insights obtained through a combination of atomistic simulations and biophysical measurements that are synthesized into a coherent framework using polymer physics theories.
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Cites
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Self-citationA quantitative measure for protein conformational heterogeneity
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“In addition, their ensembles are expected to display significant conformational heterogeneity [39] as characterized by spontaneous conformational fluctuations whose amplitudes are likely to be considerably larger than those of globular proteins.”
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Cited by
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“As most IDPs are polyampholytes (Das et al., 2015), modifications to SLiM flanking regions modulating their charge state (by e.g., phosphorylation) may induce transitions in the conformational ensemble of the disordered chain enabling allosteric regulation of motif accessibility ( Figure 1F ).”
BackgroundConformational buffering underlies functional selection in intrinsically disordered protein regions
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Metadata
- Authors
- Das, R. K., Ruff, K. M., & Pappu, R. V.
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2015-06
- Volume
- 32
- Pages
- 102-112
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W1972376083
- Cited by
- 413
- References
- 6
- FWCI
- 2.48
- Type
- journal article
- Language
- en
- Open access
- green
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