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  Improved validation of IDP ensembles by one-bond Cα-Hα scalar couplings.

Gapsys, V., Narayanan, R. L., Xiang, S., de Groot, B. L., & Zweckstetter, M. (2015). Improved validation of IDP ensembles by one-bond Cα-Hα scalar couplings. Journal of Biomolecular NMR, 63(3), 299-307. doi:10.1007/s10858-015-9990-z.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-09D8-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-19A4-6
Genre: Journal Article

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 Creators:
Gapsys, V.1, Author              
Narayanan, R. L.2, Author              
Xiang, S.3, Author              
de Groot, B. L.1, Author              
Zweckstetter, M.2, Author              
Affiliations:
1Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578573              
2Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              
3Research Group of Solid-State NMR-2, MPI for Biophysical Chemistry, Max Planck Society, ou_1950286              

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Free keywords: Ensemble; Intrinsically disordered protein; NMR; Scalar coupling
 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)JCalphaHalpha 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)JCalphaHalpha values and protein backbone dihedral angles. We show that accurate amino-acid specific random coil values of the (1)JCαHα coupling constant, in combination with a reparameterized empirical Karplus-type equation, allow for reliable cross-validation of molecular ensembles of IDPs.

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Language(s): eng - English
 Dates: 2015-10-032015-11
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1007/s10858-015-9990-z
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Title: Journal of Biomolecular NMR
Source Genre: Journal
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Pages: - Volume / Issue: 63 (3) Sequence Number: - Start / End Page: 299 - 307 Identifier: -