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Dangerous liaisons between detergents and membrane proteins. The case of mitochondrial uncoupling protein 2. Exchange of substrates across the inner membrane of mitochondria, a prerequisite for the production of energy in living cells, is mediated by a family of dedicated proteins possessing homologous sequences and common structural features. The so-called mitochondrial carrier family suffers from a paucity of structural information, barring one notable exception, the ADP/ATP carrier (AAC), for which a high-resolution structure is available. Associating low-resolution NMR data with molecular-fragment replacement, a three-dimensional structure of isoform 2 of an uncoupling protein (UCP2) binding an inhibitor was recently obtained in dodecylphosphocholine detergent micelles. Although this structure shares common traits with AAC, its functional and biological significance remains to be addressed. In the present investigation, we combine experimental and theoretical approaches to demonstrate cogently that dodecylphosphocholine severely alters the structure and, hence, the function of UCP. The proposed original strategy opens new vistas for probing the physiological relevance of three-dimensional structures of membrane proteins obtained in non-native environments. J. Am. Chem. Soc. 2013.

Recent publications

Comer, J.; Schulten, K.; Chipot, C.
Calculation of lipid-bilayer permeabilities using an average force
J.Chem. Theory Comput.
  2014, 10 (2), 554-564.
dx.doi.org

Marquardt, R.; Hénin, J.; Dehez, F.; Chipot, C.,
Dynamiques moléculaires quantiques et classiques
L’Actualité Chimique
  2014,  (382-383), 56-62.

Comer, J.; Roux, B.; Chipot, C.;
Achieving ergodic sampling using replica-exchange free-energy calculations
Mol. Sim.
  2014, 40 (1-3),  218-228.
dx.doi.org

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