A Structure-free Method for Quantifying Conformational Flexibility in proteins
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A structure-free.pdf
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860.87 KB
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Author(s)
Arenas, Daniel J.
Burger, Virginia
Stultz, Collin M
Date Issued
June 2016
Journal
Scientific Reports
Publisher
Nature Publishing Group
Citation
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
Version
Final published version
Abstract
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.
MIT Department
Massachusetts Institute of Technology. Department of Electrical Engineering and Computer Science
Massachusetts Institute of Technology. Research Laboratory of Electronics
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Creative Commons Attribution 4.0 International License
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DOI of Published Version
https://doi.org/10.1038/srep29040
