Natively unfolded proteins are increasingly recognized to play important physiological roles. These proteins do not crystallize, so NMR is the only technique able to provide structural and dynamic information. However, in unfolded proteins, the proton chemical shift dispersion is poor, causing severe problems in resonance assignment. We designed a novel strategy based on two protonless experiments, a CBCACON-IPAP and a novel COCON-IPAP, that permits a straightforward and unequivocal backbone heteronuclear assignment of the natively unfolded protein alpha-synuclein.

Protonless NMR experiments for sequence-specific assignment of backbone nuclei in unfolded proteins / W.Bermel; I.Bertini; I.C.Felli; Y.M.Lee; C.Luchinat; R.Pierattelli. - In: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY. - ISSN 0002-7863. - STAMPA. - 128:(2006), pp. 3918-3919. [10.1021/ja0582206]

Protonless NMR experiments for sequence-specific assignment of backbone nuclei in unfolded proteins

BERTINI, IVANO;FELLI, ISABELLA CATERINA;LEE, YONG-MIN;LUCHINAT, CLAUDIO;PIERATTELLI, ROBERTA
2006

Abstract

Natively unfolded proteins are increasingly recognized to play important physiological roles. These proteins do not crystallize, so NMR is the only technique able to provide structural and dynamic information. However, in unfolded proteins, the proton chemical shift dispersion is poor, causing severe problems in resonance assignment. We designed a novel strategy based on two protonless experiments, a CBCACON-IPAP and a novel COCON-IPAP, that permits a straightforward and unequivocal backbone heteronuclear assignment of the natively unfolded protein alpha-synuclein.
2006
128
3918
3919
W.Bermel; I.Bertini; I.C.Felli; Y.M.Lee; C.Luchinat; R.Pierattelli
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/309325
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