ReviewFrontiers in molecular biosciences2015
Exploring intrinsically disordered proteins using site-directed spin labeling electron paramagnetic resonance spectroscopy.
Review in Frontiers in molecular biosciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Nitroxide spin, non-canonical amino acids and SDSL-EPR spectroscopy: a winning combination for protein dynamics studies.European biophysics journal : EBJ · 2026Article
- Toward a unified framework for determining conformational ensembles of disordered proteins.Nature methods · 2026Review
- Computational Methods to Investigate Intrinsically Disordered Proteins and their Complexes.ArXiv · 2024Article
- Illuminating Intrinsically Disordered Proteins with Integrative Structural Biology.Biomolecules · 2023Review
- Intermolecular contributions, filtration effects and signal composition of SIFTER (single-frequency technique for refocusing).Magnetic resonance (Gottingen, Germany) · 2023Article
- Site-Directed Spin Labeling EPR Spectroscopy for Determination of Albumin Structural Damage and Hypoalbuminemia in Critical COVID-19.Antioxidants (Basel, Switzerland) · 2022Article
- Molecular mechanism for the synchronized electrostatic coacervation and co-aggregation of alpha-synuclein and tau.Nature communications · 2022Article
- PP2A is activated by cytochromeComputational and structural biotechnology journal · 2022Article
- Integrative structural dynamics probing of the conformational heterogeneity in synaptosomal-associated protein 25.Cell reports. Physical science · 2021Article
- A combined NMR and EPR investigation on the effect of the disordered RGG regions in the structure and the activity of the RRM domain of FUS.Scientific reports · 2020Article
- Nickel and GTP ModulateBiomolecules · 2020Article
- Conformational Dynamics in Extended RGD-Containing Peptides.Biomacromolecules · 2020Article
- The mechanism of Hsp90-induced oligomerizaton of Tau.Science advances · 2020Article
- Entropy and Information within Intrinsically Disordered Protein Regions.Entropy (Basel, Switzerland) · 2019Article
- Double Nitroxide Labeling by Copper-Catalyzed Azide-Alkyne Cycloadditions with Noncanonical Amino Acids for Electron Paramagnetic Resonance Spectroscopy.ACS chemical biology · 2019Article
- Two Tau binding sites on tubulin revealed by thiol-disulfide exchanges.Scientific reports · 2018Article
- Analysis of the Intrinsically Disordered N-Terminus of the DNA Junction-Resolving Enzyme T7 Endonuclease I: Identification of Structure Formed upon DNA Binding.Biochemistry · 2016Article
- Dynamic Protein Interaction Networks and New Structural Paradigms in Signaling.Chemical reviews · 2016Review
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Authors and funding
7 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Proteins are highly variable biological systems, not only in their structures but also in their dynamics. The most extreme example of dynamics is encountered within the family of Intrinsically Disordered Proteins (IDPs), which are proteins lacking a well-defined 3D structure under physiological conditions. Among the biophysical techniques well-suited to study such highly flexible proteins, Site-Directed Spin Labeling combined with EPR spectroscopy (SDSL-EPR) is one of the most powerful, being able to reveal, at the residue level, structural transitions such as folding events. SDSL-EPR is based on selective grafting of a paramagnetic label on the protein under study and is limited neither by the size nor by the complexity of the system. The objective of this mini-review is to describe the basic strategy of SDSL-EPR and to illustrate how it can be successfully applied to characterize the structural behavior of IDPs. Recent developments aimed at enlarging the panoply of SDSL-EPR approaches are presented in particular newly synthesized spin labels that allow the limitations of the classical ones to be overcome. The potentialities of these new spin labels will be demonstrated on different examples of IDPs.
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