An intraresidual i(HCA)CO(CA)NH experiment for the assignment of main-chain resonances in 15N, 13C labeled proteins

Journal of Biomolecular NMR

Volumn 45, Issue 3, 2009, Pages 301-310

  Mäntylahti, Sampo ^a   Tossavainen, Helena ^a   Hellman, Maarit ^a   Permi, Perttu ^a  

^a UNIVERSITY OF HELSINKI   (Finland)

Author keywords

(HCA)CO(CA)NH; Assignment; CT16; HN(CA)CO; Proteins; Ubiquitin

Indexed keywords

CARBON 13; NITROGEN 15; UBIQUITIN;

ALPHA HELIX; ARTICLE; BETA SHEET; CONTROLLED STUDY; ISOTOPE LABELING; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PERFORMANCE MEASUREMENT SYSTEM; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN FOLDING; RESIDUE ANALYSIS; SENSITIVITY ANALYSIS; STRUCTURE ANALYSIS;

CARBON ISOTOPES; HUMANS; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEINS; UBIQUITIN;

EID: 70350343815     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-009-9373-4     Document Type: Article

References (38)

1. Alho N, Klaavuniemi T, Ylanne J, Permi P, Mattila S (2007) Backbone NMR assignment of the internal interaction site of ALP. Biomol NMR Assign 1:85-87
2. 15N-labeled proteins. J Magn Reson B 110:65-68
3. Bendall MR (1995) Heteronuclear J coupling precession during spin-lock and adiabatic pulses. Use of adiabatic inversion pulses in high-resolution NMR. J Magn Reson A116:46-58
4. 15N-labelled proteins. J Biomol NMR 27:57-67
5. Brutscher B (2002) Intraresidue HNCA and COHNCA experiments for protein backbone resonance assignment. J Magn Reson 156:155-159
6. Clubb RH, Thanabal V, Wagner G (1992) A constant-time three-dimensional triple-resonance pulse scheme to correlate intraresidue 1HN, 15N, and 13C′ chemical shifts in 15N-13C-labelled proteins. J Magn Reson 97:213-217
7. Delaglio F, Torchia DA, Bax A (1991) Measurement of 15N-13C J couplings in staphylococcal nuclease. J Biomol NMR 1:439-446
8. Dyson HJ, Wright PE (2001) Nuclear magnetic resonance methods for elucidation of structure and dynamics in disordered states. Methods Enzymol 339:258-270
9. Folmer R, Otting G (2000) Sensitivity enhancement in (HCA)CONH experiments. J Biomol NMR 16:229-233
10. Griffey RH, Redfield AG (1987) Proton-detected heteronuclear edited and correlated nuclear-magnetic-resonance and nuclear Overhauser effect in solution. Q Rev Biophys 19:51-82
11. Grzesiek S, Bax A (1992) Improved 3D triple-resonance NMR techniques applied to a 31-kDa protein. J Magn Reson 96:432-440
12. Hennig M, Ott D, Schulte P, Lowe R, Krebs J, Vorherr T, Bermel W, Schwalbe H, Griesinger C (1997) Determination of homonuclear 13C-13C J couplings between aliphatic carbon atoms in perdeuterated proteins. J Am Chem Soc 119:5055-5056
13. N) coupling constants in proteins. J Am Chem Soc 122:6268-6277
14. Hu JS, Bax A (1996) Measurement of three-bond 13C-13C J couplings between carbonyl and carbonyl/carboxyl carbons in isotopically enriched proteins. J Am Chem Soc 118:8170-8171
15. 13C three-bond J couplings measured by three-dimensional heteronuclear NMR. How planar is the peptide bond? J Am Chem Soc 119:6360-6368
16. Hu JS, Bax A (1998) Measurement of three-bond, 13C′-13Cb J couplings in human ubiquitin by a triple resonance, E.COSY-type NMR technique. J Biomol NMR 11:199-203
17. Jaravine VA, Zhuravleva AV, Permi P, Ibraghimov I, Orekhov VY (2008) Hyperdimensional NMR spectroscopy with nonlinear sampling. J Am Chem Soc 130:3927-3936
18. Jiang L, Coggins BE, Zhou P (2005) Rapid assignment of protein side chain resonances using projection-reconstruction of (4, 3)D HC(CCO)NH and intra-HC(C)NH experiments. J Magn Reson 175:170-176
19. Kay LE, Ikura M, Tschudin R, Bax A (1990) Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins. J Magn Reson 89:496-514
20. Kay LE, Keifer P, Saarinen T (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J Am Chem Soc 114:10663-10665
21. Kupće E, Wagner G (1995) Wideband homonuclear decoupling in protein spectra. J Magn Reson 109A:329-333
22. Lescop E, Schanda P, Rasia R, Brutscher B (2007) Automated spectral compression for fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy. J Am Chem Soc 129:2756-2767
23. Löhr F, Rüterjans H (1995) A New triple-resonance experiment for the sequential assignment of backbone resonances in proteins. J Biomol NMR 6:189-197
24. Marion D, Ikura M, Tschudin R, Bax A (1989) Rapid recording of 2D NMR-spectra without phase cycling - application to the study of hydrogen-exchange in proteins. J Magn Reson 85:393-399
25. Muhandiram DR, Kay LE (1994) Gradient-enhanced triple-resonance NMR experiments with improved sensitivity. J Magn Reson B103:203-216
26. Nietlispach D (2004) A selective intra-HN(CA)CO experiment for the backbone assignment of deuterated proteins. J Biomol NMR 28:131-136
27. Nietlispach D, Ito Y, Laue ED (2002) A novel approach for the sequential backbone assignment of larger proteins: Selective intra-HNCA and DQ-HNCA. J Am Chem Soc 124:11199-11207
28. Permi P (2002) Intraresidual HNCA: An experiment for correlating only intraresidual backbone resonances. J Biomol NMR 23:201-209
29. Permi P, Annila A (2004) Coherence transfer in proteins. Prog Nucl Magn Reson Spectr 44:97-137
30. 15N spins in proteins. Magn Reson Chem 44:168-176
31. Sattler M, Schleucher J, Griesinger C (1999) Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog Nucl Magn Reson Spectr 34:93-158
32. Sayers EW, Torchia DA (2001) Use of the carbonyl chemical shift to relieve degeneracies in triple-resonance assignment experiments. J Magn Reson 153:246-253
33. Shaka AJ, Lee CJ, Pines A (1988) Iterative schemes for bilinear operators - application to spin decoupling. J Magn Reson 77:274-293
34. Silver MS, Joseph RJ, Hoult DI (1984) Highly selective φ2 and π pulse generation. J Magn Reson 59:347-351
35. Tessari M, Gentile LN, Taylor SJ, Shalloway DI, Nicholson LK, Vuister G (1997) Heteronuclear NMR studies of the combined Src homology domains 2 and 3 of pp60 c-Src: Effects of phosphopeptide binding. Biochemistry 36:14561-14571
36. Tossavainen H, Permi P (2004) Optimized pathway selection in intraresidual triple-resonance experiments. J Magn Reson 170:244-251
37. 2H labeled proteins with high-sensitivity. J Am Chem Soc 116:11655-11666
38. Yao J, Dyson HJ, Wright PE (1997) Chemical shift dispersion and secondary structure prediction in unfolded and partly folded proteins. FEBS Lett 419:285-289