Improved validation of IDP ensembles by one-bond CÎ±â??HÎ± scalar couplings

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Improved validation of IDP ensembles by one-bond CÎ±â??HÎ± scalar couplings

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10-04-2015, 02:58 PM

nmrlearner

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Improved validation of IDP ensembles by one-bond CÎ±â??HÎ± scalar couplings

Improved validation of IDP ensembles by one-bond CÎ±â??HÎ± scalar couplings

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 1JCÎ±HÎ± coupling constant is particularly suited for cross-validation, because it has a large magnitude and mostly depends on the often less accessible dihedral angle Ï?. Here, we reinvestigated the connection between 1JCÎ±HÎ± values and protein backbone dihedral angles. We show that accurate amino-acid specific random coil values of the 1JCÎ±HÎ± coupling constant, in combination with a reparameterized empirical Karplus-type equation, allow for reliable cross-validation of molecular ensembles of IDPs.

Source: Journal of Biomolecular NMR

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