Improving Coarse-Grained Protein Force Fields with Small-Angle X-ray Scattering Data
Name
AWSEM-SAXS.pdf
Description
Accepted version
Size
5.12 MB
Format
Adobe PDF
Checksum (MD5)
7ff614f6788464d54b0e8da08206bcfd
Author(s)
Latham, Andrew P
Zhang, Bin
Date Issued
February 2019
Journal
Journal of Physical Chemistry B
Publisher
American Chemical Society (ACS)
Citation
Latham, Andrew P., and Bin Zhang. "Improving Coarse-Grained Protein Force Fields with Small-Angle X-ray Scattering Data." Journal of Physical Chemistry B 123, 5 (February 2019): 957-1214 doi 10.1021/ACS.JPCB.8B10336 ©2019 Author(s)
Version
Author's final manuscript
Abstract
Small-angle X-ray scattering (SAXS) experiments provide valuable structural data for biomolecules in solution. We develop a highly efficient maximum entropy approach to fit SAXS data by introducing minimal biases to a coarse-grained protein force field, the associative memory, water mediated, structure, and energy model (AWSEM). We demonstrate that the resulting force field, AWSEM-SAXS, succeeds in reproducing scattering profiles and models protein structures with shapes that are in much better agreement with experimental results. Quantitative metrics further reveal a modest, but consistent, improvement in the accuracy of modeled structures when SAXS data are incorporated into the force field. Additionally, when applied to a multiconformational protein, we find that AWSEM-SAXS is able to recover the population of different protein conformations from SAXS data alone. We, therefore, conclude that the maximum entropy approach is effective in fine-tuning the force field to better characterize both protein structure and conformational fluctuation.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
Terms of Use
Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
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DOI of Published Version
https://doi.org/10.1021/ACS.JPCB.8B10336
