CT-13C H(CCO)NH, (H)C(CO)NH, H(CCO)NH-TOCSY, C(CCO)NH-TOCSY (G. Montelione, Rutgers Univ.)

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Name: pfg_C_hacaconh_se12
Synopsis: family of HC(CO)NH straight-through triple resonance experiments; constant time 13C evolution, with sensitivity enhancement option

Code authors:

 C.B. Rios, M. Tashiro, W. Feng, G.T. Montelione
Copyright: G.T. Montelione, Protein NMR Laboratory - Center for Advanced Biotechnology and Medicine, Rutgers University
Console: Varian, Inc. Unity, 500 MHz
Console requirements: four RF channels (applies to some CABM sequences)
Source: CABM Pulse Sequence Library
Download (external links):readme pulse sequence parameters (tar) figure (pdf)

References

  1. Montelione, GT and Lyons, BA and Emerson, SD and Tashiro, M. An efficient triple resonance experiment using carbon-13 isotropic mixing for determining sequence-specific resonance assignments of isotopically-enriched proteins. Journal of the American Chemical Society 114(27):10974--10975, 1992. BibTeX [monte92]

  2. Lyons, BA and Tashiro, M and Cedergren, L and Bilsson, B and Montelione, GT. An improved strategy for determining resonance assignments for isotopically enriched proteins and its application to an engineered domain of staphylococcal protein A. Biochemistry 32(31):7839--7845, 1993. BibTeX [lyons93]

  3. Tashiro, M and Rios, CB and Montelione, GT. Classification of amino acid spin systems using PFG HCC (CO) NH-TOCSY with constant-time aliphatic 13 C frequency labeling. Journal of Biomolecular NMR 6(2):211--216, 1995. BibTeX [tash95]

  4. Feng, W and Rios, CB and Montelione, GT. Phase labeling of C- H and C- C spin-system topologies: Application in PFG-HACANH and PFG-HACA (CO) NH triple-resonance experiments for determining backbone resonance assignments in proteins. Journal of Biomolecular NMR 8(1):98--104, 1996. BibTeX [feng96]

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