Structure Determination in “Shiftless” Solid State NMR of Oriented Protein Samples

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Structure Determination in “Shiftless” Solid State NMR of Oriented Protein Samples


Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 20 June 2011

Yuanyuan, Yin , Alexander A., Nevzorov

An efficient formalism for calculating protein structures from oriented-sample NMR data in the torsion-angle space is presented. Angular anisotropies of the NMR observables are treated by utilizing an irreducible spherical basis of rotations. An intermediate rotational transformation is introduced that greatly speeds up structural fitting by rendering the dependence on the torsion angles ? and ? in a purely diagonal form. Back-calculation of the simulated solid-state NMR spectra of protein G involving 15N chemical shift anisotropy (CSA), and 1H-15N and 1H?-13C? dipolar couplings was performed by taking into account non-planarity of the peptide linkages and experimental uncertainty. Even a relatively...

Graphical abstract

*Graphical abstract:*Structure calculations from ‘shiftless’ solid-state NMR data of oriented protein samples: choice for the molecular frame, and back calculation of structures based entirely on three dipolar couplings per peptide plane*Highlights:*? An algorithm for calculating structures of oriented protein samples entirely from the dipolar couplings is presented ? Non-planarity of peptide linkages is included ? Effect of experimental uncertainty is assessed ? Structures of protein G and a helical hairpin from bacteriorhodopsin are calculated from synthetic spectra




Source: Journal of Magnetic Resonance