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A 4D HCCH-TOCSY experiment for assigning the side chain1H and13C resonances of proteins
Authors:Edward T Olejniczak  Robert X Xu  Stephen W Fesik
Institution:(1) Pharmaceutical Discovery Division, Abbott Laboratories, 60064 Abbott Park, IL, USA
Abstract:Summary A 4D HCCH-TOCSY experiment is described for correlating and assigning the1H and13C resonances of protein amino acid side chains that has several advantages over 3D versions of the experiment. In many cases, both the1H and13C chemical shifts can be obtained in the 4D experiment from a simple inspection of the13C(ohgr3),1H(ohgr4) planes extracted at the1Hagr(ohgr1)/13Cagr(ohgr2) chemical shifts. Together with the 3D and 4D triple resonance experiments, this allows sequence-specific assignments to be obtained. In addition, the increased resolution of the 4D experiment compared to its 3D counterpart allows. automation of resonance assignments.
Keywords:4D NMR  HCCH-TOCSY  Side-chain resonance assignments  Proteins
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