본문 바로가기
HOME> 논문 > 논문 검색상세

논문 상세정보

Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy v.174, 2017년, pp.223 - 229   SCI SCIE
본 등재정보는 저널의 등재정보를 참고하여 보여주는 베타서비스로 정확한 논문의 등재여부는 등재기관에 확인하시기 바랍니다.

Tyrosine fluorescence probing of conformational changes in tryptophan-lacking domain of albumins

Zhdanova, N.G. (Department of Physics, M.V. Lomonosov Moscow State University, 119991, Russia ) ; Maksimov, E.G. (Department of Biology, M.V. Lomonosov Moscow State University, 119991, Russia ) ; Arutyunyan, A.M. (A.N. Belozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, 119991, Russia ) ; Fadeev, V.V. (Department of Physics, M.V. Lomonosov Moscow State University, 119991, Russia ) ; Shirshin, E.A. (Department of Physics, M.V. Lomonosov Moscow State University, 119991, Russia ) ;
  • 초록  

    Abstract We addressed the possibility of using tyrosine (Tyr) fluorescence for monitoring conformational changes of proteins which are undetectable via tryptophan (Trp) fluorescence. The model objects, human (HSA) and bovine (BSA) serum albumins, contain one and two Trp residues, respectively, while Tyr is more uniformly distributed over their structure. The results of the investigation of albumins interaction with ethanol using intrinsic Trp and Tyr steady-state and time-resolved picosecond fluorescence indicated the presence of an intermediate at 10% (v/v) of ethanol in solution, that was supported by the results of extrinsic fluorescence measurements with the Nile Red dye. Based on the comparison of HSA and BSA Trp and Tyr fluorescence, it was suggested that conformational changes at low ethanol concentration are located in the domain III of albumins, which lacks tryptophan residues. The sensitivity of Tyr fluorescence to domain III alterations was further verified by studying albumins interaction with GdnHCl. Highlights Tyr fluorescence was used to monitor conformation of albumin with EtOH and GdnHCl. Tyr-Trp fluorescence diagram reveals intermediates in protein folding. Tyrosine fluorescence is sensitive to changes in domain III of albumin. Graphical Abstract [DISPLAY OMISSION]


  • 주제어

    Albumin .   Conformational changes .   Tyrosine fluorescence .   Fluorescence lifetime .   Fluorescence spectroscopy.  

 활용도 분석

  • 상세보기

    amChart 영역
  • 원문보기

    amChart 영역

원문보기

무료다운로드
  • 원문이 없습니다.

유료 다운로드의 경우 해당 사이트의 정책에 따라 신규 회원가입, 로그인, 유료 구매 등이 필요할 수 있습니다. 해당 사이트에서 발생하는 귀하의 모든 정보활동은 NDSL의 서비스 정책과 무관합니다.

원문복사신청을 하시면, 일부 해외 인쇄학술지의 경우 외국학술지지원센터(FRIC)에서
무료 원문복사 서비스를 제공합니다.

NDSL에서는 해당 원문을 복사서비스하고 있습니다. 위의 원문복사신청 또는 장바구니 담기를 통하여 원문복사서비스 이용이 가능합니다.

이 논문과 함께 출판된 논문 + 더보기