Academic Journal
Structural Flexibility of Tau in Its Interaction with Microtubules as Viewed by Site-Directed Spin Labeling EPR Spectroscopy
| العنوان: | Structural Flexibility of Tau in Its Interaction with Microtubules as Viewed by Site-Directed Spin Labeling EPR Spectroscopy |
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| المؤلفون: | Martinho, Marlène, Allegro, Diane, Etienne, Emilien, Lohberger, Cynthia, Bonucci, Alessio, Belle, Valérie, Barbier, Pascale |
| المساهمون: | Bioénergétique et Ingénierie des Protéines (BIP ), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Institut de neurophysiopathologie (INP) |
| المصدر: | ISSN: 1064-3745. |
| بيانات النشر: | HAL CCSD Humana Press/Springer Imprint |
| سنة النشر: | 2024 |
| المجموعة: | Aix-Marseille Université: HAL |
| مصطلحات موضوعية: | Electron Paramagnetic Resonance, Fuzzy complex, Intrinsically Disordered Proteins, Microtubules, Nitroxide radical, Site-Directed Spin Labeling, Spin labels, Tau proteinTauprotein, Tubulin dimers, [SDV]Life Sciences [q-bio], [PHYS.PHYS.PHYS-BIO-PH]Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph] |
| الوصف: | International audience ; Tau is a microtubule-associated protein that belongs to the Intrinsically Disordered Proteins (IDPs) family. IDPs or Intrinsically Disordered Regions (IDRs) play key roles in protein interaction networks and their dysfunctions are often related to severe diseases. Defined by their lack of stable secondary and tertiary structures in physiological conditions while being functional, these proteins use their inherent structural flexibility to adapt to and interact with various binding partners. Knowledges on the structural dynamics of IDPs and their different conformers are crucial to finely decipher fundamental biological processes controlled by mechanisms such as conformational adaptations or switches, induced fit, or conformational selection events. Different mechanisms of binding have been proposed: among them, the so-called folding-upon-binding in which the IDP adopts a certain conformation upon interacting with a partner protein, or the formation of a "fuzzy" complex in which the IDP partly keeps its dynamical character at the surface of its partner. The dynamical nature and physicochemical properties of unbound as well as bound IDPs make this class of proteins particularly difficult to characterize by classical bio-structural techniques and require specific approaches for the fine description of their inherent dynamics.Among other techniques, Site-Directed Spin Labeling combined with Electron Paramagnetic Resonance (SDSL-EPR) spectroscopy has gained much interest in this last decade for the study of IDPs. SDSL-EPR consists in grafting a paramagnetic label (mainly a nitroxide radical) at selected site(s) of the macromolecule under interest followed by its observation using and/or combining different EPR strategies. These nitroxide spin labels detected by continuous wave (cw) EPR spectroscopy are used as perfect reporters or "spy spins" of their local environment, being able to reveal structural transitions, folding/unfolding events, etc. Another approach is based on the measurement of ... |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| Relation: | info:eu-repo/semantics/altIdentifier/pmid/38512660; hal-04519239; https://amu.hal.science/hal-04519239; PUBMED: 38512660 |
| DOI: | 10.1007/978-1-0716-3629-9_3 |
| الاتاحة: | https://amu.hal.science/hal-04519239 https://doi.org/10.1007/978-1-0716-3629-9_3 |
| رقم الانضمام: | edsbas.B57EBF28 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1007/978-1-0716-3629-9_3 |
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