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Volumn 57, Issue 1, 2013, Pages 57-63

Direct correlation of consecutive C′-N groups in proteins: A method for the assignment of intrinsically disordered proteins

Author keywords

13C detected experiments; Backbone assignment; Intrinsically disordered proteins; Multidimensional NMR

Indexed keywords

CARBON 13; CARBONYL DERIVATIVE; NITROGEN 15; NUPR 1 PROTEIN; PROTEIN; UNCLASSIFIED DRUG;

EID: 84883551151     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-013-9765-3     Document Type: Article
Times cited : (23)

References (32)
  • 2
    • 67349216108 scopus 로고    scopus 로고
    • H-start for exclusively heteronuclear NMR spectroscopy: The case of intrinsically disordered proteins
    • 2009JMagR.198.275B 10.1016/j.jmr.2009.02.012
    • Bermel W, Bertini I, Csizmok V, Felli IC, Pierattelli R, Tompa P (2009a) H-start for exclusively heteronuclear NMR spectroscopy: the case of intrinsically disordered proteins. J Magn Reson 198:275-281
    • (2009) J Magn Reson , vol.198 , pp. 275-281
    • Bermel, W.1    Bertini, I.2    Csizmok, V.3    Felli, I.C.4    Pierattelli, R.5    Tompa, P.6
  • 5
    • 84868115572 scopus 로고    scopus 로고
    • Exclusively heteronuclear 13C-detected amino-acid-selective NMR experiments for the study of intrinsically disordered proteins (IDP)
    • Bermel W, Bertini I, Chill J, Felli IC, Haba N, Kumar V, Pieratelli R (2012b) Exclusively heteronuclear 13C-detected amino-acid-selective NMR experiments for the study of intrinsically disordered proteins (IDP). Chem Biochem 13:2425-2432
    • (2012) Chem Biochem , vol.13 , pp. 2425-2432
    • Bermel, W.1    Bertini, I.2    Chill, J.3    Felli, I.C.4    Haba, N.5    Kumar, V.6    Pieratelli, R.7
  • 7
    • 33745042221 scopus 로고    scopus 로고
    • Alanine check points in HNN and HN(C)N spectra
    • 2006JMagR.181.21C 10.1016/j.jmr.2006.03.009
    • Chatterjee A, Kumar A, Hosur RV (2006) Alanine check points in HNN and HN(C)N spectra. J Magn Reson 181:21-28
    • (2006) J Magn Reson , vol.181 , pp. 21-28
    • Chatterjee, A.1    Kumar, A.2    Hosur, R.V.3
  • 8
    • 38349049191 scopus 로고    scopus 로고
    • Tuning the HNN experiment: Generation of serine-threonine check points
    • 10.1007/s10858-007-9217-z
    • Chugh J, Kumar D, Hosur RV (2008) Tuning the HNN experiment: generation of serine-threonine check points. J Biomol NMR 40:145-152
    • (2008) J Biomol NMR , vol.40 , pp. 145-152
    • Chugh, J.1    Kumar, D.2    Hosur, R.V.3
  • 9
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • 10.1007/BF00197809
    • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277-293
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 11
    • 0034912536 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for elucidation of structure and dynamics in disordered states
    • 10.1016/S0076-6879(01)39317-5
    • Dyson HJ, Wright PE (2001) Nuclear magnetic resonance methods for elucidation of structure and dynamics in disordered states. Methods Enzymol 339:258-270
    • (2001) Methods Enzymol , vol.339 , pp. 258-270
    • Dyson, H.J.1    Wright, P.E.2
  • 12
    • 4344707281 scopus 로고    scopus 로고
    • Unfolded proteins and protein folding studied by NMR
    • 10.1021/cr030403s
    • Dyson HJ, Wright PE (2004) Unfolded proteins and protein folding studied by NMR. Chem Rev 104:3607-3622
    • (2004) Chem Rev , vol.104 , pp. 3607-3622
    • Dyson, H.J.1    Wright, P.E.2
  • 13
    • 60349087841 scopus 로고    scopus 로고
    • Biophysical characterization of intrinsically disordered proteins
    • 10.1016/j.sbi.2008.12.004
    • Eliezer D (2009) Biophysical characterization of intrinsically disordered proteins. Curr Opin Struct Biol 19:23-30
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 23-30
    • Eliezer, D.1
  • 14
    • 13844255387 scopus 로고    scopus 로고
    • Natively unfolded proteins
    • 10.1016/j.sbi.2005.01.002
    • Fink AL (2005) Natively unfolded proteins. Curr Opin Struct Biol 15:35-41
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 35-41
    • Fink, A.L.1
  • 15
    • 0000061511 scopus 로고
    • 15N-enriched proteins. Application to triple resonance 4D J connectivity of sequential amides
    • 10.1021/ja00063a068
    • 15N-enriched proteins. Application to triple resonance 4D J connectivity of sequential amides. J Am Chem Soc 115:4369-4370
    • (1993) J Am Chem Soc , vol.115 , pp. 4369-4370
    • Grzesiek, S.1    Anglister, J.2    Ren, J.H.3    Bax, A.4
  • 16
    • 34249765651 scopus 로고
    • NMR view: A computer program for the visualization and analysis of NMR data
    • 10.1007/BF00404272
    • Johnson BA, Blevins RA (1994) NMR view: a computer program for the visualization and analysis of NMR data. J Biomol NMR 4:603-614
    • (1994) J Biomol NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 18
    • 77954762400 scopus 로고    scopus 로고
    • HA-detected experiments for the backbone assignment of intrinsically disordered proteins
    • 10.1007/s10858-010-9421-0
    • Mäntylahti S, Aito O, Hellman M, Permi P (2010) HA-detected experiments for the backbone assignment of intrinsically disordered proteins. J Biomol NMR 47:171-181
    • (2010) J Biomol NMR , vol.47 , pp. 171-181
    • Mäntylahti, S.1    Aito, O.2    Hellman, M.3    Permi, P.4
  • 19
    • 79954431523 scopus 로고    scopus 로고
    • Extension of the HA-detection based approach: (HCA)CON(CA)H and (HCA)NCO(CA)H experiments for the main-chain assignment of intrinsically disordered proteins
    • 10.1007/s10858-011-9470-z
    • Mäntylahti S, Hellman M, Permi P (2011) Extension of the HA-detection based approach: (HCA)CON(CA)H and (HCA)NCO(CA)H experiments for the main-chain assignment of intrinsically disordered proteins. J Biomol NMR 49:99-109
    • (2011) J Biomol NMR , vol.49 , pp. 99-109
    • Mäntylahti, S.1    Hellman, M.2    Permi, P.3
  • 22
    • 84865187352 scopus 로고    scopus 로고
    • 4D Non-uniformly sampled HCBCACON and 1 J(NCα)-selective-HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins
    • 10.1007/s10858-012-9631-8
    • Novácek J, Haba NY, Chill JH, Žídek L, Sklenár V (2012) 4D Non-uniformly sampled HCBCACON and 1 J(NCα)-selective-HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins. J Biomol NMR 53:139-148
    • (2012) J Biomol NMR , vol.53 , pp. 139-148
    • Novácek, J.1    Haba, N.Y.2    Chill, J.H.3    Žídek, L.4    Sklenár, V.5
  • 23
    • 0034919873 scopus 로고    scopus 로고
    • 15N) labeled proteins: Application to unfolded proteins
    • 10.1023/A:1011239023422
    • 15N) labeled proteins: application to unfolded proteins. J Biomol NMR 20:135-147
    • (2001) J Biomol NMR , vol.20 , pp. 135-147
    • Panchal, S.C.1    Bavesh, N.S.2    Hosur, R.V.3
  • 24
    • 71049140420 scopus 로고    scopus 로고
    • Aliasing in reduced dimensionality spectra: (3,2)D HNHA and (4,2)D HN(COCA)NH as examples
    • 10.1007/s10858-009-9383-2
    • Pantoja-Uceda D, Santoro J (2009) Aliasing in reduced dimensionality spectra: (3,2)D HNHA and (4,2)D HN(COCA)NH as examples. J Biomol NMR 45:351-356
    • (2009) J Biomol NMR , vol.45 , pp. 351-356
    • Pantoja-Uceda, D.1    Santoro, J.2
  • 25
  • 26
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • 10.1016/S0079-6565(98)00025-9
    • 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 Spectrosc 34:93-158
    • (1999) Prog Nucl Magn Reson Spectrosc , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 27
    • 27644462754 scopus 로고    scopus 로고
    • 15N-HSQC peaks using high-resolution 3D HNcocaNH experiments with non-uniform sampling
    • 10.1007/s10858-005-1284-4
    • 15N-HSQC peaks using high-resolution 3D HNcocaNH experiments with non-uniform sampling. J Biomol NMR 33:43-50
    • (2005) J Biomol NMR , vol.33 , pp. 43-50
    • Sun, Z.J.1    Frueh, D.P.2    Selenko, P.3    Hoch, J.C.4    Wagner, G.5
  • 28
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • 10.1016/S0968-0004(02)02169-2
    • Tompa P (2002) Intrinsically unstructured proteins. Trends Biochem Sci 27:527-533
    • (2002) Trends Biochem Sci , vol.27 , pp. 527-533
    • Tompa, P.1
  • 29
    • 79958044914 scopus 로고    scopus 로고
    • Unstructural biology coming of age
    • 10.1016/j.sbi.2011.03.012
    • Tompa P (2011) Unstructural biology coming of age. Curr Opin Struct Biol 21:419-425
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 419-425
    • Tompa, P.1
  • 30
    • 84870057622 scopus 로고    scopus 로고
    • Intrinsically disordered proteins: A 10-year recap
    • 10.1016/j.tibs.2012.08.004
    • Tompa P (2012) Intrinsically disordered proteins: a 10-year recap. Trends Biochem Sci 37:509-516
    • (2012) Trends Biochem Sci , vol.37 , pp. 509-516
    • Tompa, P.1
  • 31
    • 0031451750 scopus 로고    scopus 로고
    • Chemical shift dispersion and secondary structure prediction in unfolded and partially folded proteins
    • 10.1016/S0014-5793(97)01474-9
    • Yao J, Dyson HJ, Wright PE (1997) Chemical shift dispersion and secondary structure prediction in unfolded and partially folded proteins. FEBS Lett 419:285-289
    • (1997) FEBS Lett , vol.419 , pp. 285-289
    • Yao, J.1    Dyson, H.J.2    Wright, P.E.3
  • 32
    • 0031064317 scopus 로고    scopus 로고
    • Triple-resonance NOESY-based experiments with improved spectral resolution: Applications to structural characterization of unfolded, partially folded and folded proteins
    • 10.1023/A:1018658305040
    • Zhang O, Forman-Kay JD, Shortle D, Kay LE (1997) Triple-resonance NOESY-based experiments with improved spectral resolution: applications to structural characterization of unfolded, partially folded and folded proteins. J Biomol NMR 9:181-200
    • (1997) J Biomol NMR , vol.9 , pp. 181-200
    • Zhang, O.1    Forman-Kay, J.D.2    Shortle, D.3    Kay, L.E.4


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