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We have demonstrated the unrecognized versatility and potential of the previously described HNN and HN(C)N experiments to obtain residue specific peak patterns in the spectra of the (15N, 13C) labeled proteins during backbone resonance assignment. This modification leads to the rapid resonance assignment of backbone amide protons and nitrogens. HNN-ST along with HNN and HNN-A [and similarly HN(C)N-ST along with HN(C)N and HN(C)N-A] provides a substantial boost to the assignment process by scanning the scattered glycines, alanines, serines, and threonines in the protein sequence under study. The peak patterns obtained in the neighborhood of these four amino acids in the protein chain would be very helpful for assignment of large proteins because of increased number of anchor points along the sequence. Moreover, in the light of more and more unfolded/denatured proteins being getting attention worldwide because of several important reports of intrinsically unfolded proteins, in vivo, the main strength of HNN suite of experiments, as against the standard triple resonance experiments, is to deal with these unfolded proteins. More details are available at Journal of Biomolecular NMR; 2008, 40(2), 145-52
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| Date/Time | User | Dimensions | File size | Comment | |
|---|---|---|---|---|---|
| current | 22:34, 8 April 2008 | JC (Talk | contribs) | 41 KB | We have demonstrated the unrecognized versatility and potential of the previously described HNN and HN(C)N experiments to obtain residue specific peak patterns in the spectra of the (15N, 13C) labeled proteins during backbone resonance assignment. This mo |
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