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Volumn 122, Issue 6, 2000, Pages 1241-1242

The use of differential chemical shifts for determining the binding site location and orientation of protein-bound ligands [14]

Author keywords

[No Author keywords available]

Indexed keywords

ASCOMYCIN; FK 506 BINDING PROTEIN; LIGAND; PROTEIN BAK; PROTEIN BCL X; TACROLIMUS;

EID: 0034673316     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja993921m     Document Type: Letter
Times cited : (109)

References (19)
  • 9
    • 0342349850 scopus 로고    scopus 로고
    • note
    • 15N carrier at 117 ppm, 8 scans, 175 × 512 points, 1 h). Nearly complete aromatic and amide assignment was accomplished from 2D HSQC spectra for all complexes whereas only a partial assignment of the aliphatic region was achieved due to a larger signal overlap. All spectra were acquired on a Bruker DRX 800 spectrometer.
  • 10
    • 0342349853 scopus 로고    scopus 로고
    • note
    • Upon binding of ascomycin, more than 90% of FKBP amide signals display nitrogen shifts larger than 0.15 ppm or proton shifts larger than 0.03 ppm.
  • 13
    • 0343655023 scopus 로고    scopus 로고
    • note
    • L protein.
  • 14
    • 0343655022 scopus 로고    scopus 로고
    • note
    • Using differential chemical shifts, it is possible to orient the ligands into the protein binding pocket when the series of ligands bind in a similar conformation and induce the same conformational changes in the protein. In those cases in which the ligands bind differently, chemical shift differences in a larger region of the protein would be expected, allowing these ligands to be quickly identified.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.