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Volumn 135, Issue 35, 2013, Pages 12924-12927

Detection of dihydrofolate reductase conformational change by fret using two fluorescent amino acids

Author keywords

[No Author keywords available]

Indexed keywords

CONCENTRATION-DEPENDENT; CONFORMATIONAL CHANGE; DIHYDROFOLATE REDUCTASE; FLUORESCENT SPECIES; LABELED PROTEINS; REACTION COORDINATES; RESONANCE ENERGY TRANSFER; STERIC ACCESSIBILITY;

EID: 84883681327     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja403007r     Document Type: Article
Times cited : (56)

References (38)
  • 11
    • 0022973842 scopus 로고
    • While dye-quencher pairs have been employed over distances of potential utility for studying protein dynamics, the observed changes in fluorescence intensity can also be due to changes in the local environment of the donor or adventitious quenching induced by species commonly encountered in experimental settings, such as oxygen, iodine and acrylamide. See: Phillips, S. R.; Wilson, L. J.; Borkman, R. F. Curr. Eye Res. 1986, 5, 611
    • (1986) Curr. Eye Res. , vol.5 , pp. 611
    • Phillips, S.R.1    Wilson, L.J.2    Borkman, R.F.3
  • 38
    • 84873741680 scopus 로고    scopus 로고
    • DHFRs putatively containing 1 or 2 at position 17 were digested with trypsin (see: Maini, R.; Nguyen, D. T.; Chen, S.; Dedkova, L. M.; Chowdhury, S. R.; Alcana-Torano, R.; Hecht, S. M. Bioorg. Med. Chem. 2013, 21, 1088), and the expected unique typtic fragments corresponding to DHFR amino acids 13-32 were observed at m/z 2473.9 (calcd 2474) or 2420.3 (calcd 2420), respectively (Table S3)
    • (2013) Bioorg. Med. Chem. , vol.21 , pp. 1088
    • Maini, R.1    Nguyen, D.T.2    Chen, S.3    Dedkova, L.M.4    Chowdhury, S.R.5    Alcana-Torano, R.6    Hecht, S.M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.