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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

Research output: Contribution to journalArticlepeer-review

70 Citations (Scopus)
19 Downloads (Pure)

Abstract

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
Volume290
Issue number13
Early online date4 Feb 2015
DOIs
Publication statusPublished - 27 Mar 2015

Keywords

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

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