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High‐Resolution Solid‐State NMR Studies on Uniformly [ 13 C, 15 N]‐Labeled Ubiquitin
Author(s) -
Seidel Karsten,
Etzkorn Manuel,
Heise Henrike,
Becker Stefan,
Baldus Marc
Publication year - 2005
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200500085
Subject(s) - solid state nuclear magnetic resonance , biomolecule , magic angle spinning , nmr spectra database , chemistry , carbon 13 nmr , chemical shift , nuclear magnetic resonance spectroscopy , molecular dynamics , carbon 13 nmr satellite , crystallography , intermolecular force , chemical physics , analytical chemistry (journal) , fluorine 19 nmr , computational chemistry , nuclear magnetic resonance , spectral line , molecule , stereochemistry , physics , organic chemistry , biochemistry , astronomy
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 [ 13 C, 15 N]‐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 13 C′, 13 Cα, and 13 Cβ resonance frequencies suggests that 13 C 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.