|Title||Prediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins.|
|Publication Type||Journal Article|
|Year of Publication||2017|
|Authors||Shen, Y, Roche, J, Grishaev, A, Bax, A|
|Date Published||2017 Sep 08|
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.
|Alternate Journal||Protein Sci.|