A simple method to measure 13CH2 heteronuclear dipolar cross-correlation spectral densities.
Here, we report a method to simultaneously determine CH2 cross-correlation spectral densities and T1 relaxation times in the laboratory and rotating frames. To accomplish this, we have employed an indirect approach that is based on measurement of differences in relaxation rates acquired with and without cross-correlation terms. The new method, which can be employed using multidimensional NMR and standard relaxation pulse sequences, is validated experimentally by investigation of a selectively 13C-enriched hexadecapeptide and the uniformly 13C-enriched immunoglobulin-binding domain of streptococcal protein G (GB1). Use of this approach makes determination of CH2 cross-correlation spectral densities in uniformly 13C-enriched proteins now routine and provides novel information concerning their internal motions.
Idiyatullin
Djaudat
D
Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota Health Science Center, 321 Church Street, Minneapolis, MN 55455, USA.
Daragan
Vladimir A
VA
Mayo
Kevin H
KH
D001426:Bacterial Proteins / Q000032:analysis*; D002247:Carbon Isotopes; D006859:Hydrogen / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010455:Peptides / Q000032:analysis*; D012815:Signal Processing, Computer-Assisted
D001426:Bacterial Proteins; D002247:Carbon Isotopes; C034284:IgG Fc-binding protein, Streptococcus; D010455:Peptides; D006859:Hydrogen