Campus Units

Biochemistry, Biophysics and Molecular Biology, Roy J. Carver Department of, Chemistry

Document Type

Article

Publication Version

Published Version

Publication Date

1-26-2018

Journal or Book Title

Nature Communications

Volume

9

Issue

1

First Page

384

DOI

10.1038/s41467-017-02592-z

Abstract

Automated methods for NMR structure determination of proteins are continuously becoming more robust. However, current methods addressing larger, more complex targets rely on analyzing 6–10 complementary spectra, suggesting the need for alternative approaches. Here, we describe 4D-CHAINS/autoNOE-Rosetta, a complete pipeline for NOE-driven structure determination of medium- to larger-sized proteins. The 4D-CHAINS algorithm analyzes two 4D spectra recorded using a single, fully protonated protein sample in an iterative ansatz where common NOEs between different spin systems supplement conventional through-bond connectivities to establish assignments of sidechain and backbone resonances at high levels of completeness and with a minimum error rate. The 4D-CHAINS assignments are then used to guide automated assignment of long-range NOEs and structure refinement in autoNOE-Rosetta. Our results on four targets ranging in size from 15.5 to 27.3 kDa illustrate that the structures of proteins can be determined accurately and in an unsupervised manner in a matter of days.

Comments

This article is published as Evangelidis, Thomas, Santrupti Nerli, Jiří Nováček, Andrew E. Brereton, P. Andrew Karplus, Rochelle R. Dotas, Vincenzo Venditti, Nikolaos G. Sgourakis, and Konstantinos Tripsianes. "Automated NMR resonance assignments and structure determination using a minimal set of 4D spectra." Nature Communications 9, no. 1 (2018): 384. DOI: 10.1038/s41467-017-02592-z. Posted with permission.

Creative Commons License

Creative Commons Attribution 4.0 License
This work is licensed under a Creative Commons Attribution 4.0 License.

Copyright Owner

The Author(s)

Language

en

File Format

application/pdf

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