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Updated: Jun 25, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Comparative analysis of NMR chemical shift predictions for proteins in the solid phase
Karsten Seidel1, Manuel Etzkorn, Robert Schneider
1Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Abstract:
A comparative analysis of nuclear chemical shift predictions of proteins in the solid state by rapid algorithms trained on and verified with solution-state NMR assignments is presented. The precision of predictions by four dedicated computer programs (SHIFTS, PROSHIFTS, SHIFTX and SPARTA) was found to be close to values obtained for proteins in solution. Correlation coefficients depend on the NMR nucleus (N, C', C(alpha) and C(beta)) and on secondary structure (beta-strand, random coil and alpha-helix), but also on the molecular environment (membrane-integral or not). The findings establish a quantitative basis for using chemical shift prediction programs for solid-state NMR applications. On the other hand, prediction inaccuracies identified for certain resonance kind, residue type, and molecular environment point to possible areas of methodological improvement.
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