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13C-Detection
13C-detection in biomolecular NMR
The availability of 13C-observe CryoProbes™ has made it possible to develop 13C-observe methods for paramagnetic proteins and large deuterated proteins - which are otherwise difficult to study by NMR due to rapid relaxation and the absence of proton signals.
more on CryoProbes
The use of CryoProbes helps to alleviate the major disadvantage of 13C-detection, that is, the lack of sensitivity. Although 13C-detection, compared to 1H-detection, suffers from lower sensitivity, it also has a number of advantages.
Some of these include:
- Favorable relaxation behavior due to shorter pulse sequences
- Detection of non-protonated carbons
- High dispersion of 13C chemical shifts
- Absence of dominant signals from the solvent or buffer
- High salt tolerance
These properties make the 13C-detected experiments a potentially useful complement to the traditional proton detection.
2D constant time 13C-13C-TOCSY spectrum (above diagonal) and 2D real time 13C-13C-TOCSY spectrum (below diagonal) of the uniformly 2H,13C,15N-labeled trimeric 44kDa enzyme chorismate mutase from Bacillus subtilis. The measuring time for the constant time experiment was 96 hours and that of the real time experiment was 36 hours. CryoProbe optimized for 13C-detection at 500MHz was used.
Courtesy: Alexander Eletsky, Osvaldo Moreira, Helena Kovacs and Konstantin Pervushin, J. Biomol. NMR 26 (2003) 167-179.A novel strategy for the assignment of side-chain resonances in completely deuterated large proteins using 13C spectroscopy

