title: Selective diagonal-free (13)C, (13)C-edited aliphatic-aromatic NOESY experiment with non-uniform sampling.
abstract: A band-selective aromatic-aliphatic C,C-edited four-dimensional NOESY experiment is proposed here. Its key advantage is the absence of auto-correlation signals which makes it very attractive for joint use with non-uniform sampling. It is demonstrated here that the sensitivity of the experiment is not significantly affected by utilization of selective pulses (for either aromatic-13C or aliphatic-13C spins). The method was applied to the sample of E32Q mutant of human S100A1 protein, a homodimer of total molecular mass ~20 kDa. High-resolution 4D spectra were obtained from ~1.5 % of sampling points required conventionally. It is shown that superior resolution facilitates unambiguous assignment of observed aliphatic-aromatic cross-peaks. Additionally, the addition of aliphatic-13C dimension enables to resolve peaks with degenerated aliphatic (1)H chemical shifts. All observed cross-peaks were validated against previously determined 3D structure of E32Q mutant of S100A1 protein (PDB 2LHL). The increased reliability of structural constraints obtained from the proposed high-resolution 4D 13C(ali),13C(aro)-edited NOESY can be exploited in the automated protocols of structure determination of proteins.
authors: Faculty of Chemistry, University of Warsaw, Pasteura 1, 02093, Warsaw, Poland.
authors: Jan
authors: J
authors: Stanek
authors: Michał
authors: M
authors: Nowakowski
authors: Saurabh
authors: S
authors: Saxena
authors: Katarzyna
authors: K
authors: Ruszczyńska-Bartnik
authors: Andrzej
authors: A
authors: Ejchart
authors: Wiktor
authors: W
authors: Koźmiński
mesh_terms: D002247:Carbon Isotopes; D006801:Humans; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D015203:Reproducibility of Results
chemical_list: D002247:Carbon Isotopes; D011506:Proteins
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