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

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


Abstract A pair of 4D NMR experiments for the backbone assignment of disordered proteins is presented. The experiments exploit 13C direct detection and non-uniform sampling of the indirectly detected dimensions, and provide correlations of the aliphatic proton (Hα, and Hβ) and carbon (Cα, Cβ) 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 (Hα, Cα, Cβ, C�, and N) can be extracted from each spectrum. Compared to the commonly used assignment strategy based on matching the Cα and Cβ chemical shifts, inclusion of the Hα and Hβ 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.

• Content Type Journal Article
• Category Article
• Pages 1-10
• DOI 10.1007/s10858-012-9631-8
• Authors
  • JiÅ?Ã* NováÄ?ek, Faculty of Science, NCBR, and CEITEC, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic
  • Noam Y. Haba, Department of Chemistry, Bar Ilan University, Ramat Gan, 52900 Israel
  • Jordan H. Chill, Department of Chemistry, Bar Ilan University, Ramat Gan, 52900 Israel
  • Lukáš ŽÃ*dek, Faculty of Science, NCBR, and CEITEC, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic
  • VladimÃ*r SklenáÅ?, Faculty of Science, NCBR, and CEITEC, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic

• • Journal Journal of Biomolecular NMR
  • Online ISSN 1573-5001
  • Print ISSN 0925-2738

Source: Journal of Biomolecular NMR