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Default High-resolution solid-state NMR studies on uniformly [13C,15N]-labeled ubiquitin.

High-resolution solid-state NMR studies on uniformly [13C,15N]-labeled ubiquitin.

Related Articles High-resolution solid-state NMR studies on uniformly [13C,15N]-labeled ubiquitin.

Chembiochem. 2005 Sep;6(9):1638-47

Authors: Seidel K, Etzkorn M, Heise H, Becker S, Baldus M

Understanding of the effects of intermolecular interactions, molecular dynamics, and sample preparation on high-resolution magic-angle spinning NMR data is currently limited. Using the example of a uniformly [13C,15N]-labeled sample of ubiquitin, we discuss solid-state NMR methods tailored to the construction of 3D molecular structure and study the influence of solid-phase protein preparation on solid-state NMR spectra. A comparative analysis of 13C', 13Calpha, and 13Cbeta resonance frequencies suggests that 13C chemical-shift variations are most likely to occur in protein regions that exhibit an enhanced degree of molecular mobility. Our results can be refined by additional solid-state NMR techniques and serve as a reference for ongoing efforts to characterize the structure and dynamics of (membrane) proteins, protein complexes, and other biomolecules by high-resolution solid-state NMR.

PMID: 16094694 [PubMed - indexed for MEDLINE]



Source: PubMed
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