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Volumn 98, Issue 10, 2010, Pages 2043-2044

Mapping the conformational mobility of multidomain proteins

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EID: 77952694236     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.03.005     Document Type: Article
Times cited : (5)

References (6)
  • 1
    • 33847795359 scopus 로고    scopus 로고
    • Intrinsic disorder and functional proteomics
    • Radivojac, P., L. M. Iakoucheva, ..., A. K. Dunker. 2007. Intrinsic disorder and functional proteomics. Biophys. J. 92: 1439-1456.
    • (2007) Biophys. J. , vol.92 , pp. 1439-1456
    • Radivojac, P.1    Iakoucheva, L.M.2    Dunker, A.K.3
  • 2
    • 4344624612 scopus 로고    scopus 로고
    • NMR studies of modular protein structures and their interactions
    • Pickford, A. R., and I. D. Campbell. 2004. NMR studies of modular protein structures and their interactions. Chem. Rev. 104: 3557-3566.
    • (2004) Chem. Rev. , vol.104 , pp. 3557-3566
    • Pickford, A.R.1    Campbell, I.D.2
  • 4
    • 69849103777 scopus 로고    scopus 로고
    • Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings
    • Jensen, M. R., P. R. L. Markwick, ..., M. Blackledge. 2009. Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings. Structure. 17: 1169-1185.
    • (2009) Structure. , vol.17 , pp. 1169-1185
    • Jensen, M.R.1    Markwick, P.R.L.2    Blackledge, M.3
  • 5
    • 0037165750 scopus 로고    scopus 로고
    • General framework for studying the dynamics of folded and nonfolded proteins by NMR relaxation spectroscopy and MD simulation
    • Prompers, J. J., and R. Brüschweiler. 2002. General framework for studying the dynamics of folded and nonfolded proteins by NMR relaxation spectroscopy and MD simulation. J. Am. Chem. Soc. 124: 4522-4534.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 4522-4534
    • Prompers, J.J.1    Brüschweiler, R.2
  • 6
    • 84883598626 scopus 로고    scopus 로고
    • Structure and dynamics of ribosomal protein L12: An ensemble model based on SAXS and NMR relaxation
    • Bernado, P., K. Modig, ..., M. Akke. 2010. Structure and dynamics of ribosomal protein L12: an ensemble model based on SAXS and NMR relaxation. Biophys. J. 98: 2374-2382.
    • (2010) Biophys. J. , vol.98 , pp. 2374-2382
    • Bernado, P.1    Modig, K.2    Akke, M.3


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