A Structure-free Method for Quantifying Conformational Flexibility in proteins
Author(s)Arenas, Daniel J.; Burger, Virginia; Stultz, Collin M
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All proteins sample a range of conformations at physiologic temperatures and this inherent flexibility enables them to carry out their prescribed functions. A comprehensive understanding of protein function therefore entails a characterization of protein flexibility. Here we describe a novel approach for quantifying a protein’s flexibility in solution using small-angle X-ray scattering (SAXS) data. The method calculates an effective entropy that quantifies the diversity of radii of gyration that a protein can adopt in solution and does not require the explicit generation of structural ensembles to garner insights into protein flexibility. Application of this structure-free approach to over 200 experimental datasets demonstrates that the methodology can quantify a protein’s disorder as well as the effects of ligand binding on protein flexibility. Such quantitative descriptions of protein flexibility form the basis of a rigorous taxonomy for the description and classification of protein structure.
DepartmentMassachusetts Institute of Technology. Department of Electrical Engineering and Computer Science; Massachusetts Institute of Technology. Research Laboratory of Electronics
Nature Publishing Group
Burger, Virginia M., Daniel J. Arenas, and Collin M. Stultz. “A Structure-Free Method for Quantifying Conformational Flexibility in Proteins.” Scientific Reports 6.1 (2016): n. pag. © 2017 Macmillan Publishers Limited
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