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Capturing dynamic conformational shifts in protein-ligand recognition using integrative structural biology in solution.

Emerg. Top. Life Sci. 2, 107-119 (2018)
DOI Verlagsversion bestellen
In recent years, a dynamic view of the structure and function of biological macromolecules is emerging, highlighting an essential role of dynamic conformational equilibria to understand molecular mechanisms of biological functions. The structure of a biomolecule, i.e. protein or nucleic acid in solution, is often best described as a dynamic ensemble of conformations, rather than a single structural state. Strikingly, the molecular interactions and functions of the biological macromolecule can then involve a shift between conformations that pre-exist in such an ensemble. Upon external cues, such population shifts of pre-existing conformations allow gradually relaying the signal to the downstream biological events. An inherent feature of this principle is conformational dynamics, where intrinsically disordered regions often play important roles to modulate the conformational ensemble. Unequivocally, solution-state NMR spectroscopy is a powerful technique to study the structure and dynamics of such biomolecules in solution. NMR is increasingly combined with complementary techniques, including fluorescence spectroscopy and small angle scattering. The combination of these techniques provides complementary information about the conformation and dynamics in solution and thus affords a comprehensive description of biomolecular functions and regulations. Here, we illustrate how an integrated approach combining complementary techniques can assess the structure and dynamics of proteins and protein complexes in solution.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Review
Schlagwörter Nmr Spectroscopy ; Eukaryotic Gene Expression Gene Expression ; Fluorescence Resonance Energy Transfer ; Protein Dynamics ; Small Angle-based Scattering
ISSN (print) / ISBN 2397-8562
Quellenangaben Band: 2, Heft: 1, Seiten: 107-119 Artikelnummer: , Supplement: ,
Verlag Portland Press
Verlagsort London
Begutachtungsstatus Peer reviewed