Improved validation of IDP ensembles by one-bond C alpha-H alpha scalar couplings

2015 | journal article. A publication with affiliation to the University of Göttingen.

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​Improved validation of IDP ensembles by one-bond C alpha-H alpha scalar couplings​
Gapsys, V. ; Narayanan, R. L.; Xiang, S.; de Groot, B. L.   & Zweckstetter, M. ​ (2015) 
Journal of Biomolecular NMR63(3) pp. 299​-307​.​ DOI: https://doi.org/10.1007/s10858-015-9990-z 

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Authors
Gapsys, Vytautas ; Narayanan, Raghavendran L.; Xiang, ShengQi; de Groot, Bert L. ; Zweckstetter, Markus 
Abstract
Intrinsically disordered proteins (IDPs) are best described by ensembles of conformations and a variety of approaches have been developed to determine IDP ensembles. Because of the large number of conformations, however, cross-validation of the determined ensembles by independent experimental data is crucial. The (1)J(C alpha H alpha) coupling constant is particularly suited for cross-validation, because it has a large magnitude and mostly depends on the often less accessible dihedral angle psi. Here, we reinvestigated the connection between (1)J(C alpha H alpha) values and protein backbone dihedral angles. We show that accurate amino-acid specific random coil values of the (1)J(C alpha H alpha) coupling constant, in combination with a reparameterized empirical Karplus-type equation, allow for reliable cross-validation of molecular ensembles of IDPs.
Issue Date
2015
Status
published
Publisher
Springer
Journal
Journal of Biomolecular NMR 
ISSN
1573-5001; 0925-2738
Sponsor
DFG [ZW71/8-1]

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