메뉴 건너뛰기




Volumn 22, Issue 22, 2006, Pages 2833-2834

SCAssign: A sparky extension for the NMR resonance assignment of aliphatic side-chains of uniformly 13C,15N-labeled large proteins

Author keywords

[No Author keywords available]

Indexed keywords

CARBON 13; HEMOGLOBIN; MALTOSE BINDING PROTEIN; NITROGEN 15;

EID: 33751021695     PISSN: 13674803     EISSN: 13674811     Source Type: Journal    
DOI: 10.1093/bioinformatics/btl477     Document Type: Article
Times cited : (4)

References (7)
  • 1
    • 0028019827 scopus 로고
    • Multidimensional nuclear magnetic resonance methods for protein studies
    • Bax,A. (1994) Multidimensional nuclear magnetic resonance methods for protein studies. Curr. Opin. Struct. Biol., 4, 738-744.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 738-744
    • Bax, A.1
  • 2
    • 0037269913 scopus 로고    scopus 로고
    • Determination of protein global folds using backbone residual dipolar coupling and long-range NOE restraints
    • Giesen,A.W. et al. (2003) Determination of protein global folds using backbone residual dipolar coupling and long-range NOE restraints. J. Biomol. NMR, 25, 63-71.
    • (2003) J. Biomol. NMR , vol.25 , pp. 63-71
    • Giesen, A.W.1
  • 3
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • Pervushin,K. et al. (1997) Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc. Natl Acad. Sci. USA, 94, 12366-12371.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 12366-12371
    • Pervushin, K.1
  • 4
    • 0030596171 scopus 로고    scopus 로고
    • Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N and 1H assignments of human carbonic anhydrase II
    • Venters,R.A. et al. (1996) Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N and 1H assignments of human carbonic anhydrase II. J. Mol. Biol., 264, 1101-1116.
    • (1996) J. Mol. Biol. , vol.264 , pp. 1101-1116
    • Venters, R.A.1
  • 5
    • 24144499401 scopus 로고    scopus 로고
    • A general strategy for the assignment of aliphatic side-chain resonances of uniformly 13C,15N-labeled large proteins
    • Xu,Y. et al. (2005) A general strategy for the assignment of aliphatic side-chain resonances of uniformly 13C,15N-labeled large proteins. J. Am. Chem. Soc., 127, 11920-11921.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 11920-11921
    • Xu, Y.1
  • 6
    • 0033599567 scopus 로고    scopus 로고
    • TROSY triple-resonance four-dimensional NMR spectroscopy of a 46 ns tumbling protein
    • Yang,D. and Kay,L.E. (1999) TROSY triple-resonance four-dimensional NMR spectroscopy of a 46 ns tumbling protein. J. Am. Chem. Soc., 121, 2571-2575.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2571-2575
    • Yang, D.1    Kay, L.E.2
  • 7
    • 1642309196 scopus 로고    scopus 로고
    • Sequence-specific assignments of methyl groups in highmolecular weight proteins
    • Yang,D. et al. (2004) Sequence-specific assignments of methyl groups in highmolecular weight proteins. J. Am. Chem. Soc., 126, 3710-3711.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3710-3711
    • Yang, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.