Sparsely sampled high-resolution 4-D experiments for efficient backbone resonance assignment of disordered proteins.

Journal Article (Journal Article)

Intrinsically disordered proteins (IDPs) play important roles in many critical cellular processes. Due to their limited chemical shift dispersion, IDPs often require four pairs of resonance connectivities (H(α), C(α), C(β) and CO) for establishing sequential backbone assignment. Because most conventional 4-D triple-resonance experiments share an overlapping C(α) evolution period, combining existing 4-D experiments does not offer an optimal solution for non-redundant collection of a complete set of backbone resonances. Using alternative chemical shift evolution schemes, we propose a new pair of 4-D triple-resonance experiments--HA(CA)CO(CA)NH/HA(CA)CONH--that complement the 4-D HNCACB/HN(CO)CACB experiments to provide complete backbone resonance information. Collection of high-resolution 4-D spectra with sparse sampling and FFT-CLEAN processing enables efficient acquisition and assignment of complete backbone resonances of IDPs. Importantly, because the CLEAN procedure iteratively identifies resonance signals and removes their associating aliasing artifacts, it greatly reduces the dependence of the reconstruction quality on sampling schemes and produces high-quality spectra even with less-than-optimal sampling schemes.

Full Text

Duke Authors

Cited Authors

  • Wen, J; Wu, J; Zhou, P

Published Date

  • March 2011

Published In

Volume / Issue

  • 209 / 1

Start / End Page

  • 94 - 100

PubMed ID

  • 21277815

Pubmed Central ID

  • PMC3048770

Electronic International Standard Serial Number (EISSN)

  • 1096-0856

Digital Object Identifier (DOI)

  • 10.1016/j.jmr.2010.12.012


  • eng

Conference Location

  • United States