Sandbox Reserved 508: Difference between revisions

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2. A neutral fatty acid is flipped through the mitochondrial membrane into the matrix, and because of the basic environment, it releases the proton (H+). The now negatively charged anion is then transported
2. A neutral fatty acid is flipped through the mitochondrial membrane into the matrix, and because of the basic environment, it releases the proton (H+). The now negatively charged anion is then transported
through the membrane by UCP2.]]
through the membrane by UCP2.]]
[[Image:BCSMART_11-12_Figure_5.JPG|left|375px|thumb|'''FIGURE 5: UCP2 Protein Structure'''
<br>
UCP2 is an inner mitochondrial membrane protein consisting of 6 transmembrane helices, shown in
orange, with both the N- and C- termini pointing to the inter membrane space. UCP2 activity is inhibited
by nucleotide binding (eg. GDP). Lys141 and Arg185, which are speculated to bind to GDP, are
shown in light sky blue.]]
[[Image:BCSMART_11-12_Figure_6.JPG|right|375px|thumb|'''FIGURE 6: View of UCP2 Down the Barrel'''
<br>
View from matrix side through the putative transport path of UCP2. Our model may support the mechanism
where a protonated fatty acid flips through the inner membrane into the matrix, loses its proton
due to the basic interior environment, and is attracted to the matrix side by positively charged residues
(navy). Additional positively charged residues in the interior of the barrel may pass the fatty acid anion
towards the inter membrane space.]]
==References==
==References==
Berardi, M. J., Shih, W. M., Harrison, S. C., & Chou, J. J. (2011, August 4). Mitochondrial uncoupling protein 2 structure determined by
Berardi, M. J., Shih, W. M., Harrison, S. C., & Chou, J. J. (2011, August 4). Mitochondrial uncoupling protein 2 structure determined by
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