메뉴 건너뛰기




Volumn 172, Issue 2, 2005, Pages 324-328

A selective experiment for the sequential protein backbone assignment from 3D heteronuclear spectra

Author keywords

13C Direct detection; 13C NMR; Protein structure; Protonless NMR; Sequential assignment

Indexed keywords

PROTEIN STRUCTURE; PROTONLESS NMR; SEQUENTIAL ASSIGNMENT;

EID: 11344281375     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmr.2004.11.005     Document Type: Article
Times cited : (32)

References (17)
  • 1
    • 0037774524 scopus 로고    scopus 로고
    • A strategy for the NMR characterization of type II copper(II) proteins: The case of the copper trafficking protein CopC from Pseudomonas syringae
    • F. Arnesano, L. Banci, I. Bertini, I.C. Felli, C. Luchinat, and A.R. Thompsett A strategy for the NMR characterization of type II copper(II) proteins: the case of the copper trafficking protein CopC from Pseudomonas syringae J. Am. Chem. Soc. 125 2003 7200 7208
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 7200-7208
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Felli, I.C.4    Luchinat, C.5    Thompsett, A.R.6
  • 4
    • 2342512067 scopus 로고    scopus 로고
    • Strategy for the study of paramagnetic proteins with slow electronic relaxation rates by NMR spectroscopy application to oxidized human [2Fe-2S]ferredoxin
    • 2+-containing acireductome dioxygenase J. Am. Chem. Soc. 124 2002 9054 9055
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 5413-5426
    • MacHonkin, T.E.1    Westler, W.M.2    Markley, J.L.3
  • 6
    • 4344659734 scopus 로고    scopus 로고
    • Direct carbon detection in paramagnetic metalloproteins to further exploit pseudocontact shift restraints
    • E. Babini, I. Bertini, F. Capozzi, I.C. Felli, M. Lelli, and C. Luchinat Direct carbon detection in paramagnetic metalloproteins to further exploit pseudocontact shift restraints J. Am. Chem. Soc. 126 2004 10496 10497
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 10496-10497
    • Babini, E.1    Bertini, I.2    Capozzi, F.3    Felli, I.C.4    Lelli, M.5    Luchinat, C.6
  • 7
    • 5844348565 scopus 로고
    • Magnetic resonance for non rotating fields
    • F. Bloch, and A. Siegert Magnetic resonance for non rotating fields Phys. Rev. 57 1940 522 527
    • (1940) Phys. Rev. , vol.57 , pp. 522-527
    • Bloch, F.1    Siegert, A.2
  • 8
    • 0001252215 scopus 로고
    • Phase-shifts induced by transient Bloch-Siegert effect in NMR
    • L. Emsley, and G. Bodenhausen Phase-shifts induced by transient Bloch-Siegert effect in NMR Chem. Phys. Lett. 168 1990 297 303
    • (1990) Chem. Phys. Lett. , vol.168 , pp. 297-303
    • Emsley, L.1    Bodenhausen, G.2
  • 9
    • 44049117010 scopus 로고
    • Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein
    • S. Grzesiek, and A. Bax Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein J. Magn. Reson. 96 1992 432 440
    • (1992) J. Magn. Reson. , vol.96 , pp. 432-440
    • Grzesiek, S.1    Bax, A.2
  • 10
    • 11144285454 scopus 로고    scopus 로고
    • Solution structure of human β-parvalbumin and structural comparison with its paralog α-parvalbumin and with their rat orthologs
    • in press
    • E. Babini, I. Bertini, F. Capozzi, C. Del Bianco, D. Holleder, T. Kiss, C. Luchinat, A. Quattrone, Solution structure of human β-parvalbumin and structural comparison with its paralog α-parvalbumin and with their rat orthologs. Biochemistry (in press)
    • Biochemistry
    • Babini, E.1    Bertini, I.2    Capozzi, F.3    Del Bianco, C.4    Holleder, D.5    Kiss, T.6    Luchinat, C.7    Quattrone, A.8
  • 11
    • 13444269041 scopus 로고
    • Computer-optimized decoupling scheme for wideband applications and low-level operation
    • A.J. Shaka, P.B. Barker, and R. Freeman Computer-optimized decoupling scheme for wideband applications and low-level operation J. Magn. Reson. 64 1985 547 552
    • (1985) J. Magn. Reson. , vol.64 , pp. 547-552
    • Shaka, A.J.1    Barker, P.B.2    Freeman, R.3
  • 12
    • 48749144559 scopus 로고
    • Evaluation of a new broadband decoupling sequence: WALTZ-16
    • A.J. Shaka, J. Keeler, and R. Freeman Evaluation of a new broadband decoupling sequence: WALTZ-16 J. Magn. Reson. 53 1983 313 340
    • (1983) J. Magn. Reson. , vol.53 , pp. 313-340
    • Shaka, A.J.1    Keeler, J.2    Freeman, R.3
  • 13
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • L.E. Kay, P. Keifer, and T. Saarinen Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity J. Am. Chem. Soc. 114 1992 10663 10665
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 14
    • 11544304059 scopus 로고
    • Gaussian pulse cascades: New analytical functions for rectangular selective inversion and in-phase excitation in NMR
    • L. Emsley, and G. Bodenhausen Gaussian pulse cascades: new analytical functions for rectangular selective inversion and in-phase excitation in NMR Chem. Phys. Lett. 165 1990 469 476
    • (1990) Chem. Phys. Lett. , vol.165 , pp. 469-476
    • Emsley, L.1    Bodenhausen, G.2
  • 15
    • 44949291986 scopus 로고
    • Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins
    • L.E. Kay, M. Ikura, R. Tschudin, and A. Bax Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins J. Magn. Reson. 89 1990 496 514
    • (1990) J. Magn. Reson. , vol.89 , pp. 496-514
    • Kay, L.E.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 16
    • 0035742333 scopus 로고    scopus 로고
    • A sequential HNCA NMR pulse sequence for protein backbone assignment
    • A. Meissner, and O.W. Sørensen A sequential HNCA NMR pulse sequence for protein backbone assignment J. Magn. Reson. 150 2001 100 104
    • (2001) J. Magn. Reson. , vol.150 , pp. 100-104
    • Meissner, A.1    Sørensen, O.W.2
  • 17
    • 45249127991 scopus 로고
    • Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins
    • D. Marion, M. Ikura, R. Tschudin, and A. Bax Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins J. Magn. Reson. 85 1989 393 399
    • (1989) J. Magn. Reson. , vol.85 , pp. 393-399
    • Marion, D.1    Ikura, M.2    Tschudin, R.3    Bax, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.