ArticleProtein science : a publication of the Protein Society2013
Protonation-dependent conformational variability of intrinsically disordered proteins.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed.
- Electromagnetic Field Stimulation Effects on Intrinsically Disordered Proteins and Their Role in Aging and Neurodegeneration.Journal of biomedical science and engineering · 2025Article
- MEDOC: A Fast, Scalable, and Mathematically Exact Algorithm for the Site-Specific Prediction of the Protonation Degree in Large Disordered Proteins.Journal of chemical information and modeling · 2025Article
- Effects of pH on an IDP conformational ensemble explored by molecular dynamics simulation.Biophysical chemistry · 2021Article
- Characterization of Weak Protein Domain Structure by Spin-Label Distance Distributions.Frontiers in molecular biosciences · 2021Article
- The BackMAP Python module: how a simpler Ramachandran number can simplify the life of a protein simulator.PeerJ · 2018Article
- Network representation of protein interactions: Theory of graph description and analysis.Protein science : a publication of the Protein Society · 2016Article
- Network representation of protein interactions-Experimental results.Protein science : a publication of the Protein Society · 2016Article
- Article
- High resolution 4D HPCH experiment for sequential assignment of (13)C-labeled RNAs via phosphodiester backbone.Journal of biomolecular NMR · 2015Article
- Effect of temperature on the conformation of natively unfolded protein 4E-BP1 in aqueous and mixed solutions containing trifluoroethanol and hexafluoroisopropanol.The protein journal · 2015Article
- Structure and regulatory interactions of the cytoplasmic terminal domains of serotonin transporter.Biochemistry · 2014Article
- NMR contributions to structural dynamics studies of intrinsically disordered proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Review
- Digested disorder: Quarterly intrinsic disorder digest (July-August-September, 2013).Intrinsically disordered proteins · 2014Review
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11 authors.
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Abstract
Intrinsically disordered proteins (IDPs) are characterized by substantial conformational plasticity and undergo rearrangements of the time-averaged conformational ensemble on changes of environmental conditions (e.g., in ionic strength, pH, molecular crowding). In contrast to stably folded proteins, IDPs often form compact conformations at acidic pH. The biological relevance of this process was, for example, demonstrated by nuclear magnetic resonance studies of the aggregation prone (low pH) state of α-synuclein. In this study, we report a large-scale analysis of the pH dependence of disordered proteins using the recently developed meta-structure approach. The meta-structure analysis of a large set of IDPs revealed a significant tendency of IDPs to form α-helical secondary structure elements and to preferentially fold into more compact structures under acidic conditions. The predictive validity of this novel approach was demonstrated with applications to the tumor-suppressor BASP1 and the transcription factor Tcf4.
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