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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Cover Image
Cover Image
Cryo-STX projection image showing a parasitophorous vacuole (yellow) within a human fibroblast cell, containing four Toxoplasma gondii parasites (membranes in cyan, nuclei in red and rhoptries in green). In this issue of Emerging Topics in Life Sciences, Harkiolaki et al. describe the use of Cryo-soft X-ray tomography to explore the ultrastructure of whole cells. Image kindly provided by Professor Helen Saibil (Birkbeck College, London, U.K.). For further details, see pages 81–92.
Capturing dynamic conformational shifts in protein–ligand recognition using integrative structural biology in solution
Marcellus Ubbink, Anastassis Perrakis, Hyun-Seo Kang, Michael Sattler; Capturing dynamic conformational shifts in protein–ligand recognition using integrative structural biology in solution. Emerg Top Life Sci 20 April 2018; 2 (1): 107–119. doi: https://doi.org/10.1042/ETLS20170090
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