메뉴 건너뛰기




Volumn 757, Issue , 2011, Pages 129-137

An NMR method to study protein-protein interactions

Author keywords

Cross saturation; Deuterium; Interaction; Macromolecular complex; NMR

Indexed keywords

PROTEIN;

EID: 80054734164     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-61779-166-6_10     Document Type: Article
Times cited : (8)

References (8)
  • 1
    • 0034051065 scopus 로고    scopus 로고
    • A novel NMR method for determining the interfaces of large protein- protein complexes
    • DOI 10.1038/73331
    • Takahashi, H., Nakanishi, T., Kami, K., Arata, Y., and Shimada, I. (2000) A novel NMR method for determining the interfaces of large protein-protein complexes. Nat. Struct. Biol. 7, 220-223. (Pubitemid 30140768)
    • (2000) Nature Structural Biology , vol.7 , Issue.3 , pp. 220-223
    • Takahashi, H.1    Nakanishi, T.2    Kami, K.3    Arata, Y.4    Shimada, I.5
  • 2
    • 0036302354 scopus 로고    scopus 로고
    • Determination of the interface of a large protein complex by transferred cross-saturation measurements
    • DOI 10.1016/S0022-2836(02)00018-9
    • Nakanishi, T., Miyazawa, M., Sakakura, M., Terasawa, H., Takahashi, H., and Shimada, I. (2002) Determination of the interface of a large protein complex by transferred crosssaturation measurements. J. Mol. Biol. 318, 245-249. (Pubitemid 34734823)
    • (2002) Journal of Molecular Biology , vol.318 , Issue.2 , pp. 245-249
    • Nakanishi, T.1    Miyazawa, M.2    Sakakura, M.3    Terasawa, H.4    Takahashi, H.5    Shimada, I.6
  • 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., Riek, R., Wider, G., and Wuthrich, K. (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    Riek, R.2    Wider, G.3    Wuthrich, K.4
  • 4
    • 0000377543 scopus 로고
    • Wideband homonuclear decoupling in protein spectra
    • Kupce, E., and Wagner, G. (1995) Wideband homonuclear decoupling in protein spectra. J. Magn. Res. B. 109, 329-333.
    • (1995) J. Magn. Res. B , vol.109 , pp. 329-333
    • Kupce, E.1    Wagner, G.2
  • 5
    • 0032488629 scopus 로고    scopus 로고
    • NMR study of the interaction between the B domain of staphylococcal protein A and the Fc portion of immunoglobulin G
    • DOI 10.1021/bi970923f
    • Gouda, H., Shiraishi, M., Takahashi, H., Kato, K., Torigoe, H., Arata, Y., et al. (1998) NMR study of the interaction between the B domain of staphylococcal protein A and the Fc portion of immunoglobulin G. Biochemistry 37, 129-136. (Pubitemid 28049114)
    • (1998) Biochemistry , vol.37 , Issue.1 , pp. 129-136
    • Gouda, H.1    Shiraishi, M.2    Takahashi, H.3    Kato, K.4    Torigoe, H.5    Arata, Y.6    Shimada, I.7
  • 8
    • 77955323388 scopus 로고    scopus 로고
    • Theoretical analysis of the transferred crosssaturation method
    • 139-155
    • Matsumoto, M., Ueda, T., Shimada, I. (2010) Theoretical analysis of the transferred crosssaturation method. J. Magn. Reson. 205, 114-124. 139-155
    • (2010) J. Magn. Reson , vol.205 , pp. 114-124
    • Matsumoto, M.1    Ueda, T.2    Shimada, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.