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chuwendan,xuyang,zhoucuiyan,luyafei,yuxiaoxia,zhangruixuan,liwenqi.Study of membrane protein TmrAB by Analytical Ultracentrifugation[J].Progress in Biochemistry and Biophysics
Study of membrane protein TmrAB by Analytical Ultracentrifugation
Received:July 18, 2018  Revised:August 30, 2018
Key words:Analytical Ultracentrifugation, membrane protein, Size exclusion chromatography, Cryo-SEM, protein molecular weight
Fund:中国博士后科学基金面上资助(2014M550050)
Author NameAffiliationE-mail
chuwendan School of Biomedicine in Tsinghua University chuwendan@biomed.tsinghua.edu.cn 
xuyang School of Biomedicine in Tsinghua University  
zhoucuiyan School of Biomedicine in Tsinghua University  
luyafei School of Biomedicine in Tsinghua University  
yuxiaoxia Institute of Biophysics, Chinese Academy of Sciences  
zhangruixuan School of life science, Tsinghua University  
liwenqi School of Biomedicine in Tsinghua University liwenqi@tsinghua.edu.cn 
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Abstract:
      Detergent is critical for membrane protein purification, impacting their state of oligomerization, crystallization conditions and other physicochemical properties. Analytical Ultracentrifugation (AUC), by characterizing the sedimentation of membrane protein-detergent complex in centrifugal fields, is able to measure various hydrodynamic and thermodynamic properties, including sedimentation coefficient, molar mass, hydrodynamic radius, binding coefficient, thus defining the homogeneity and oligomerization state of membrane protein-detergent complex. This study focuses on an ABC transporter from thermophilic bacteria, TmrAB, and utilizes AUC coupled to size-exclusion chromatography and negative staining electron microscopy to determine its homogeneity, oligomerization, and stoichiometry of membrane protein and detergent molecules. The results indicate that TmrAB complex exists as homogeneous monomer of heterodimers of TmrA and TmrB, in the condition of 8x Critical Micelle Concentration (CMC) DDM, having a ratio of DDM/TmrAB equal to 116:1. This study suggests, AUC is a reliable means to analyze the molecular weight of membrane protein.
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