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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April 2018
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Review Article|
April 20 2018
Capturing dynamic conformational shifts in protein–ligand recognition using integrative structural biology in solution
Hyun-Seo Kang
;
Hyun-Seo Kang
1
Institute of Structural Biology, Helmholtz Zentrum München, 85764 Neuherberg, Germany2
Center for Integrated Protein Science (CiPSM) at Biomolecular NMR, Department of Chemie, Technische Universität München, 85747 Garching, Germany
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Michael Sattler
1
Institute of Structural Biology, Helmholtz Zentrum München, 85764 Neuherberg, Germany2
Center for Integrated Protein Science (CiPSM) at Biomolecular NMR, Department of Chemie, Technische Universität München, 85747 Garching, Germany
Correspondence: Michael Sattler (sattler@helmholtz-muenchen.de)
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Emerg Top Life Sci (2018) 2 (1): 107-119.
Article history
Received:
March 05 2018
Revision Received:
March 18 2018
Accepted:
March 20 2018
Citation
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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