Trends in thermostability provide information on the nature of substrate, inhibitor, and lipid interactions with mitochondrial carriers

Paul G. Crichton, Yang Lee, Jonathan J. Ruprecht, Elizabeth Cerson, Chancievan Thangaratnarajah, Martin S. King, Edmund R. S. Kunji

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Background: Methods for rapid assessment of interactions of small molecules with membrane proteins in detergent are lacking. 

Results: Thermostability measurements of mitochondrial transporters display informative trends about detergent, lipid, substrate, and inhibitor interactions. 

Conclusion: Mechanistic insights are obtained by studying the thermostability of mitochondrial transporters. 

Significance: Information about the nature of compound interactions with membrane proteins can be obtained rapidly.

Original languageEnglish
Pages (from-to)8206-8217
Number of pages12
JournalJournal of Biological Chemistry
Issue number13
Early online date4 Feb 2015
Publication statusPublished - 27 Mar 2015


  • Membrane Protein
  • Mitochondrial Transport
  • Protein Stability
  • Transporter
  • Uncoupling Protein
  • Adenine Nucleotide Translocase
  • Detergent Micelle
  • Differential Scanning Fluorimetry
  • Thermofluor Assay

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