Synergies of Single Molecule Fluorescence and NMR for the Study of Intrinsically Disordered Proteins - Université Grenoble Alpes
Article Dans Une Revue Biomolecules Année : 2021

Synergies of Single Molecule Fluorescence and NMR for the Study of Intrinsically Disordered Proteins

Samuel Naudi-Fabra
Martin Blackledge
Sigrid Milles

Résumé

Single molecule fluorescence and nuclear magnetic resonance spectroscopy (NMR) are two very powerful techniques for the analysis of intrinsically disordered proteins (IDPs). Both techniques have individually made major contributions to deciphering the complex properties of IDPs and their interactions, and it has become evident that they can provide very complementary views on the distance-dynamics relationships of IDP systems. We now review the first approaches using both NMR and single molecule fluorescence to decipher the molecular properties of IDPs and their interactions. We shed light on how these two techniques were employed synergistically for multidomain proteins harboring intrinsically disordered linkers, for veritable IDPs, but also for liquid–liquid phase separated systems. Additionally, we provide insights into the first approaches to use single molecule Förster resonance energy transfer (FRET) and NMR for the description of multiconformational models of IDPs.

Dates et versions

hal-03549064 , version 1 (31-01-2022)

Identifiants

Citer

Samuel Naudi-Fabra, Martin Blackledge, Sigrid Milles. Synergies of Single Molecule Fluorescence and NMR for the Study of Intrinsically Disordered Proteins. Biomolecules, 2021, 12 (1), pp.27. ⟨10.3390/biom12010027⟩. ⟨hal-03549064⟩
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