Abstract
Standard methods for de novo protein structure determination by nuclear magnetic resonance (NMR) require time-consuming data collection and interpretation efforts. Here we present a qualitatively distinct and novel approach, called Comparative, Objective Measurement of Protein Architectures by Scoring Shifts (COMPASS), which identifies the best structures from a set of structural models by numerical comparison with a single, unassigned 2D 13C-13C NMR spectrum containing backbone and side-chain aliphatic signals. COMPASS does not require resonance assignments. It is particularly well suited for interpretation of magic-angle spinning solid-state NMR spectra, but also applicable to solution NMR spectra. We demonstrate COMPASS with experimental data from four proteins - GB1, ubiquitin, DsbA, and the extracellular domain of human tissue factor - and with reconstructed spectra from 11 additional proteins. For all these proteins, with molecular mass up to 25 kDa, COMPASS distinguished the correct fold, most often within 1.5 Å root-mean-square deviation of the reference structure.
Original language | English (US) |
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Pages (from-to) | 1958-1966 |
Number of pages | 9 |
Journal | Structure |
Volume | 23 |
Issue number | 10 |
DOIs | |
State | Published - Oct 6 2015 |
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology