The starting point of any standard protocol for protein-structure determination by NMR spectroscopy is the sequence-specific resonance assignment of the polypeptide chain. An experiment for determining backbone assignment starts and ends on 13C nuclei and exploits only heteronuclei. This experiment paves a new route for those cases in which the 1H lines are too severely broadened.
A heteronuclear direct-detection NMR spectroscopy experiment for protein-backbone assignment / I.Bertini; L.Duma; I.C.Felli; M.Fey; C.Luchinat; R.Pierattelli; P.R.Vasos. - In: ANGEWANDTE CHEMIE. INTERNATIONAL EDITION. - ISSN 1433-7851. - STAMPA. - 43:(2004), pp. 2257-2259. [10.1002/anie.200453661]
A heteronuclear direct-detection NMR spectroscopy experiment for protein-backbone assignment
BERTINI, IVANO;FELLI, ISABELLA CATERINA;LUCHINAT, CLAUDIO;PIERATTELLI, ROBERTA;
2004
Abstract
The starting point of any standard protocol for protein-structure determination by NMR spectroscopy is the sequence-specific resonance assignment of the polypeptide chain. An experiment for determining backbone assignment starts and ends on 13C nuclei and exploits only heteronuclei. This experiment paves a new route for those cases in which the 1H lines are too severely broadened.
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