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Measuring membrane protein stability under native conditions

Chang, Yu-Chu ; Bowie, James U

Proceedings of the National Academy of Sciences of the United States of America, 07 January 2014, Vol.111(1), pp.219-24 [Tạp chí có phản biện]

E-ISSN: 1091-6490 ; PMID: 24367094 Version:1 ; DOI: 10.1073/pnas.1318576111

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  • Nhan đề:
    Measuring membrane protein stability under native conditions
  • Tác giả: Chang, Yu-Chu ; Bowie, James U
  • Chủ đề: Membrane Protein Folding ; Steric Trap ; Micelles ; Protein Stability ; Bacteriorhodopsins -- Chemistry ; Dimyristoylphosphatidylcholine -- Chemistry ; Membrane Proteins -- Chemistry
  • Là 1 phần của: Proceedings of the National Academy of Sciences of the United States of America, 07 January 2014, Vol.111(1), pp.219-24
  • Mô tả: The thermodynamic stability of proteins is typically measured at high denaturant concentrations and then extrapolated back to zero denaturant conditions to obtain unfolding free energies under native conditions. For membrane proteins, the extrapolations are fraught with considerable uncertainty as the denaturants may have complex effects on the membrane or micellar structure. We therefore sought to measure stability under native conditions, using a method that does not perturb the properties of the membrane or membrane mimetics. We use a technique called steric trapping to measure the thermodynamic stability of bacteriorhodopsin in bicelles and micelles. We find that bacteriorhodopsin has a high thermodynamic stability, with an unfolding free energy of ∼11 kcal/mol in dimyristoyl phosphatidylcholine bicelles. Nevertheless, the stability is much lower than predicted by extrapolation of measurements made at high denaturant concentrations. We investigated the discrepancy and found that unfolding...
  • Ngôn ngữ: English
  • Số nhận dạng: E-ISSN: 1091-6490 ; PMID: 24367094 Version:1 ; DOI: 10.1073/pnas.1318576111

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