13C direct detected NMR increases the detectability of residual dipolar couplings.
13C direct detection is becoming an increasingly efficient approach to identify signals of residues that escape detection in 1H detected experiments. Pulse sequences have been developed to obtain 1H partially recoupled experiments for the measurement of the 1JHalphaCalpha and 1JHN couplings with the same resolution available in conventional 1H detected experiments. A consistent set of backbone rdc obtained without any 1H-based experiment has been obtained and shown to be effective for protein solution structure determination.
Balayssac
Stéphane
S
Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy.
Bertini
Ivano
I
Luchinat
Claudio
C
Parigi
Giacomo
G
Piccioli
Mario
M
D064026:Calbindins; D002247:Carbon Isotopes; D008667:Metalloproteins / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011522:Protons; D064030:S100 Calcium Binding Protein G / Q000737:chemistry*; D013932:Thulium / Q000737:chemistry
D064026:Calbindins; D002247:Carbon Isotopes; D008667:Metalloproteins; D011522:Protons; D064030:S100 Calcium Binding Protein G; D013932:Thulium