Fluctuations of backbone torsion angles obtained from NMR-determined structures and their prediction
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Protein molecules exhibit varying degrees of flexibility throughout their three-dimensional structures. Protein structural flexibility is often characterized by fluctuations in the Cartesian coordinate space. On the other hand, the protein backbone can be mostly defined by two torsion angles / and w only. We introduce a new flexibility descriptor, backbone torsion-angle fluctuation derived from the variation of backbone torsion angles from different NMR models. The torsion-angle fluctuations correlate with mean-squared spatial fluctuations derived from the same collection of NMR models. We developed a neural-network based real-value predictor based on sequence information only. The predictor achieved ten-fold cross-validated correlation coefficients of 0.59 and 0.60, and mean absolute errors of 22.78 and 24.38 for the angle fluctuation of / and w, respectively. This predictor is expected to be useful for function prediction and protein structure prediction when predicted torsion angles are used as restraints.
Proteins: Structure, Function, and Bioinformatics
© 2010 Wiley Periodicals, Inc. This is the accepted version of the following article: Fluctuations of backbone torsion angles obtained from NMR-determined structures and their prediction, Proteins: Structure, Function, and Bioinformatics, Vol. 78(16), 2010, pp. 3353-3362, which has been published in final form at dx.doi.org/10.1002/prot.22842.