Premium
Exclusively Heteronuclear NMR Experiments to Obtain Structural and Dynamic Information on Proteins
Author(s) -
Bermel Wolfgang,
Bertini Ivano,
Felli Isabella C.,
Peruzzini Riccardo,
Pierattelli Roberta
Publication year - 2010
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.200900772
Subject(s) - heteronuclear molecule , residual dipolar coupling , chemistry , nuclear magnetic resonance spectroscopy , transverse relaxation optimized spectroscopy , relaxation (psychology) , residual , coupling constant , macromolecule , dipole , heteronuclear single quantum coherence spectroscopy , nuclear magnetic resonance , computational chemistry , chemical physics , fluorine 19 nmr , biological system , physics , stereochemistry , organic chemistry , biochemistry , algorithm , computer science , particle physics , psychology , social psychology , biology
Provided that 13 C‐detected NMR experiments are either preferable or complementary to 1 H detection, we report here tools to determine C α C′, C′N, and C α H α residual dipolar couplings on the basis of the CON experiment. The coupling constants determined on ubiquitin are consistent with the subset measured with the 1 H‐detected HNCO sequences. Since the utilization of residual dipolar couplings may depend on the mobility of the involved nuclei, we also provide tools to measure longitudinal and transverse relaxation rates of N and C′. This new set of experiments is a further development of a whole strategy based on 13 C direct‐detection NMR spectroscopy for the study of biological macromolecules.