4D Non-uniformly sampled HCBCACON and (1) J(NC alpha)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins

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Publikace nespadá pod Lékařskou fakultu, ale pod Středoevropský technologický institut. Oficiální stránka publikace je na webu muni.cz.
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NOVÁČEK Jiří HABA Noam Y CHILL Jordan H ŽÍDEK Lukáš SKLENÁŘ Vladimír

Rok publikování 2012
Druh Článek v odborném periodiku
Časopis / Zdroj Journal of Biomolecular NMR
Fakulta / Pracoviště MU

Středoevropský technologický institut

Citace
www http://www.springerlink.com/content/g5116115mh441831/?MUD=MP
Doi http://dx.doi.org/10.1007/s10858-012-9631-8
Obor Biofyzika
Klíčová slova Intrinsically disordered proteins; Non-uniform sampling; C-13 detection; Chemical shifts; Residual secondary structure; Prolines assignment
Popis A pair of 4D NMR experiments for the backbone assignment of disordered proteins is presented. The experiments exploit C-13 direct detection and non-uniform sampling of the indirectly detected dimensions, and provide correlations of the aliphatic proton (H-alpha, and H-beta) and carbon (C-alpha, C-beta) resonance frequencies to the protein backbone. Thus, all the chemical shifts regularly used to map the transient secondary structure motifs in the intrinsically disordered proteins (H-alpha, C-alpha, C-beta, C', and N) can be extracted from each spectrum. Compared to the commonly used assignment strategy based on matching the C-alpha and C-beta chemical shifts, inclusion of the H-alpha and H-beta provides up to three extra resonance frequencies that decrease the chance of ambiguous assignment. The experiments were successfully applied to the original assignment of a 12.8 kDa intrinsically disordered protein having a high content of proline residues (26 %) in the sequence.
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