Prediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins.

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TitlePrediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins.
Publication TypeJournal Article
Year of Publication2017
AuthorsShen, Y, Roche, J, Grishaev, A, Bax, A
JournalProtein Sci
Date Published2017 Sep 08
ISSN1469-896X
Abstract

Using fine-tuned hydrogen bonding criteria, a library of coiled peptide fragments has been generated from a large set of high-resolution protein X-ray structures. This library is shown to be an improved representation of ϕ/ψ torsion angles seen in intrinsically disordered proteins (IDPs). The ϕ/ψ torsion angle distribution of the library, on average, provides good agreement with experimentally observed chemical shifts and (3) JHN-Hα coupling constants for a set of five disordered proteins. Inspection of the coil library confirms that nearest-neighbor effects significantly impact the ϕ/ψ distribution of residues in the coil state. Importantly, (3) JHN-Hα coupling constants derived from the nearest-neighbor modulated backbone ϕ distribution in the coil library show improved agreement to experimental values, thereby providing a better way to predict (3) JHN-Hα coupling constants for IDPs, and for identifying locations that deviate from fully random behavior. This article is protected by copyright. All rights reserved.

DOI10.1002/pro.3292
Alternate JournalProtein Sci.
PubMed ID28884933