Part of the Advances in Experimental Medicine and Biology book series (volume 611)
Conformational Analysis and Folding of Transmembrane and Matrix Peptide Segments of the Mitochondrial Uncoupling Proteins: A Comparative Study
The archetypal Uncoupling Protein 1(UCP-1) is a mitochondrial regulated protein carrier/ion channel, and by far the best studied isoform of the mammalian UCP subfamily of transporters located in the inner membrane of mitochondria. Thermogenic proton leak resulting in the decoupling of ATP synthesis from cellular respiration is considered to be the main physiological function of UCP-1, which is mainly found in brown adipose tissues. UCP-1 also transports anions and fatty acids. The other four mammalian UCP isoforms are located in several tissues, including brain (UCPs 4 and 5), which in addition to proton transport possess diverse physiological roles such as reduction of oxidative stress and protection against cardiac ischemia. Despite an increasing number of publications about the physiological functions of UCPs, the molecular mechanisms of the biological function as well as the structure of UCPs are not yet fully understood. To address these questions, we have...
KeywordsBrown Adipose Tissue Uncouple Protein Helical Conformation Matrix Loop Peptide Segment
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
This work was funded by CFI and NSERC grants to M.J.-N. and M.D.S.
© Springer Science+Business Media, LLC 2009