Bayesian inference of protein structure from chemical shift data

Department of Chemistry, University of Copenhagen, Copenhagen, Denmark
Department of Biology, Bioinformatics Center, University of Copenhagen, Copenhagen, Denmark
DOI
10.7287/peerj.preprints.692v1
Subject Areas
Biochemistry, Bioinformatics, Computational Biology, Computational Science
Keywords
Markov chain Monte Carlo, NMR, Probabilistic models, Protein structure, Chemical shifts
Copyright
© 2014 Bratholm et al.
Licence
This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ PrePrints) and either DOI or URL of the article must be cited.
Cite this article
Bratholm LA, Christensen AS, Hamelryck T, Jensen JH. 2014. Bayesian inference of protein structure from chemical shift data. PeerJ PrePrints 2:e692v1

Abstract

Protein chemical shifts are routinely used to augment molecular mechanics force fields in protein structure simulations, with weights of the chemical shift restraints determined empirically. These weights, however, might not be an optimal descriptor of a given protein structure and predictive model, and a bias is introduced which might result in incorrect structures. In the inferential structure determination framework, both the unknown structure and the disagreement between experimental and back-calculated data are formulated as a joint probability distribution, thus utilizing the full information content of the data. Here, we present the formulation of such a probability distribution where the error in chemical shift prediction is described by either a Gaussian or Cauchy distribution. The methodology is demonstrated and compared to a set of empirically weighted potentials through Markov chain Monte Carlo simulations of three small proteins (ENHD, Protein G and the SMN Tudor Domain) using the PROFASI force field and the chemical shift predictor CamShift. Using a clustering-criterion for identifying the best structure, together with the addition of a solvent exposure scoring term, the simulations suggests that sampling both the structure and the uncertainties in chemical shift prediction leads more accurate structures compared to conventional methods using empirical determined weights. The Cauchy distribution, using either sampled uncertainties or predetermined weights, did, however, result in overall better convergence to the native fold, suggesting that both types of distribution might be useful in different aspects of the protein structure prediction.

Author Comment

This article will be a submission to PeerJ for review.

Supplemental Information

Figures of protein structures discussed in the main text and example phaistos settings

DOI: 10.7287/peerj.preprints.692v1/supp-1

Native pdb and str (chemical shift) files used in the simulations

DOI: 10.7287/peerj.preprints.692v1/supp-2

Subset of sampled structures in pdb format, compressed in zip and subfolders in 7zip

DOI: 10.7287/peerj.preprints.692v1/supp-3