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

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F12%3A00057624" target="_blank" >RIV/00216224:14740/12:00057624 - isvavai.cz</a>
Result on the web
<a href="http://www.springerlink.com/content/g5116115mh441831/?MUD=MP" target="_blank" >http://www.springerlink.com/content/g5116115mh441831/?MUD=MP</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1007/s10858-012-9631-8" target="_blank" >10.1007/s10858-012-9631-8</a>

Result language
angličtina
Original language name
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
Original language description
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.
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
BO - Biophysics
OECD FORD branch
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Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2012
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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