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Volumn 38, Issue 12, 1999, Pages 1784-1788

Characterization of ligand binding by saturation transfer difference NMR spectroscopy

Author keywords

Bioaffinity studies; Combinatorial chemistry; Molecular recognitionn; NMR spectroscopy

Indexed keywords

EPITOPE; PROTEIN;

EID: 0033553844     PISSN: 14337851     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1521-3773(19990614)38:12<1784::AID-ANIE1784>3.0.CO;2-Q     Document Type: Article
Times cited : (1448)

References (26)
  • 1
    • 0030917461 scopus 로고    scopus 로고
    • DE-A 19649359 (international patent pending)
    • a) B. Meyer, T. Weimar, T. Peters, Eur. J. Biochem. 1997, 246, 705-709; DE-A 19649359 (international patent pending);
    • (1997) Eur. J. Biochem. , vol.246 , pp. 705-709
    • Meyer, B.1    Weimar, T.2    Peters, T.3
  • 20
    • 33747566687 scopus 로고    scopus 로고
    • note
    • 2O (cf. reference [12]). 1D NMR spectra were multiplied by an exponential line broadening function of 3 Hz prior to Fourier transformation. The irradiation power in all experiments was set to about 0.2 W.
  • 26
    • 33747521268 scopus 로고    scopus 로고
    • unpublished results
    • The mapping of binding epitopes was shown for peptides and glycopeptides binding to the SM3 monoclonal antibody specific to cancerous mucl mucines. H. Möller, N. Ötztürk, J. Taylor-Papadimitriou, H. Paulsen, B. Meyer, unpublished results.
    • Möller, H.1    Ötztürk, N.2    Taylor-Papadimitriou, J.3    Paulsen, H.4    Meyer, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.