HNCA is a 3D triple-resonance NMR experiment commonly used in the field of protein NMR . The name derives from the experiment's magnetization transfer pathway: The magnetization of the amide proton of an amino acid residue is transferred to the amide nitrogen, and then to the alpha carbons of both the starting residue and the previous residue in the protein's amino acid sequence. In contrast, the complementary HNCOCA experiment transfers magnetization only to the alpha carbon of the previous residue. The HNCA experiment is used, often in tandem with HNCOCA, to assign alpha carbon resonance signals to specific residues in the protein. This experiment requires a purified sample of protein prepared with C and N isotopic labelling , at a concentration greater than 0.1 mM , and is thus generally only applied to recombinant proteins .
6-412: The spectrum produced by this experiment has 3 dimensions: A proton axis, a N axis and a C axis. For residue i peaks will appear at {H N (i), N(i), C alpha (i)} and {H N (i), N(i), C alpha (i-1)}, while for the complementary HNCOCA experiment peaks appear only at {H N (i), N(i), C alpha (i-1)}. Together, these two experiments reveal the alpha carbon chemical shift for each amino acid residue in
12-494: A N axis and a C axis. For residue i peaks will appear at {H N (i), N(i), C α (i-1)} only, while for the complementary HNCA experiment peaks appear at {H N (i), N(i), C α (i-1)} and {H N (i), N(i), C α (i)}. Together, these two experiments reveal the alpha carbon chemical shift for each amino acid residue in a protein, and provide information linking adjacent residues in the protein's sequence. Bax A, Ikura M (May 1991). "An efficient 3D NMR technique for correlating
18-524: A protein, and provide information linking adjacent residues in the protein's sequence. Protein NMR Spectroscopy ;: Principles and Practice (1995) John Cavanagh, Wayne J. Fairbrother, Arthur G. Palmer III, Nicholas J. Skelton, Academic Press This biophysics -related article is a stub . You can help Misplaced Pages by expanding it . This protein -related article is a stub . You can help Misplaced Pages by expanding it . HNCOCA HNCOCA
24-475: Is a 3D triple-resonance NMR experiment commonly used in the field of protein NMR . The name derives from the experiment's magnetization transfer pathway: The magnetization of the amide proton of an amino acid residue is transferred to the amide nitrogen, and then to the alpha carbon of the previous residue in the protein's amino acid sequence. In contrast, the complementary HNCA experiment transfers magnetization to
30-508: The alpha carbons of both the starting residue and the previous residue in the sequence. The HNCOCA experiment is used, often in tandem with HNCA, to assign alpha carbon resonance signals to specific residues in the protein. This experiment requires a purified sample of protein prepared with C and N isotopic labelling , at a concentration greater than 0.1 mM , and is thus generally only applied to recombinant proteins . The spectrum produced by this experiment has 3 dimensions: A proton axis,
36-434: The proton and 15N backbone amide resonances with the alpha-carbon of the preceding residue in uniformly 15N/13C enriched proteins". J. Biomol. NMR . 1 (1): 99–104. doi : 10.1007/BF01874573 . PMID 1668719 . John Cavanagh; Wayne J. Fairbrother; Arthur G. Palmer III; Nicholas J. Skelton (1995). Protein NMR Spectroscopy : Principles and Practice . Academic Press . This biophysics -related article
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