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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- 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]