Other formats:
BibTeX
LaTeX
RIS
@article{1066896, author = {Nováček, Jiří and Haba, Noam Y and Chill, Jordan H and Žídek, Lukáš and Sklenář, Vladimír}, article_location = {Dordrecht}, article_number = {2}, doi = {http://dx.doi.org/10.1007/s10858-012-9631-8}, keywords = {Intrinsically disordered proteins; Non-uniform sampling; C-13 detection; Chemical shifts; Residual secondary structure; Prolines assignment}, language = {eng}, issn = {0925-2738}, journal = {Journal of Biomolecular NMR}, title = {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}, url = {http://www.springerlink.com/content/g5116115mh441831/?MUD=MP}, volume = {53}, year = {2012} }
TY - JOUR ID - 1066896 AU - Nováček, Jiří - Haba, Noam Y - Chill, Jordan H - Žídek, Lukáš - Sklenář, Vladimír PY - 2012 TI - 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 JF - Journal of Biomolecular NMR VL - 53 IS - 2 SP - 139-148 EP - 139-148 PB - Springer Netherlands SN - 09252738 KW - Intrinsically disordered proteins KW - Non-uniform sampling KW - C-13 detection KW - Chemical shifts KW - Residual secondary structure KW - Prolines assignment UR - http://www.springerlink.com/content/g5116115mh441831/?MUD=MP L2 - http://www.springerlink.com/content/g5116115mh441831/?MUD=MP N2 - 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. ER -
NOVÁČEK, Jiří, Noam Y HABA, Jordan H CHILL, Lukáš ŽÍDEK and Vladimír SKLENÁŘ. 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. \textit{Journal of Biomolecular NMR}. Dordrecht: Springer Netherlands, 2012, vol.~53, No~2, p.~139-148. ISSN~0925-2738. Available from: https://dx.doi.org/10.1007/s10858-012-9631-8.
|