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                 <p>The yeast <b><i>Saccharomyces cerevisiae</i></b> has several properties which have established it as an important tool in the expression of foreign protein for research, industrial or medical use. As a food organism, it is highly acceptable for the production of pharmaceutical proteins. In contrast, <b><i>Escherichia coli</i></b> have toxic cell wall pyroxenes and mammalian cells may contain oncogenic or viral DNA, so that products from these organisms must be tested hmore extensively.</p>

                 <p>The yeast <b><i>Saccharomyces cerevisiae</i></b> has several properties which have established it as an important tool in the expression of foreign protein for research, industrial or medical use. As a food organism, it is highly acceptable for the production of pharmaceutical proteins. In contrast, <b><i>Escherichia coli</i></b> have toxic cell wall pyroxenes and mammalian cells may contain oncogenic or viral DNA, so that products from these organisms must be tested hmore extensively.</p>

                 <p>Yeast can be grown rapidly on simple media and to high cell density and its genetics are more advanced than any other eukaryote, so that it can be manipulated almost as readily as <b><i>E.coli</i></b>. As a eukaryote, yeast is a suitable host organism for the High-level production of secreted as well as soluble cytosolic proteins.</p>

                 <p>Yeast can be grown rapidly on simple media and to high cell density and its genetics are more advanced than any other eukaryote, so that it can be manipulated almost as readily as <b><i>E.coli</i></b>. As a eukaryote, yeast is a suitable host organism for the High-level production of secreted as well as soluble cytosolic proteins.</p>

                 <p>UCP1 can transport protons through two different hypothesized mechanisms. In the first model, UCP1 transfers protons from intermembrane space to mitochondria matrix. Fatty acids provide essential free carboxy groups catalyzing proton (H+) translocation. In this model, Coenzyme Q(CoQ) serves as a necessary cofactor of UCP1, activating the protein functions.</p>

                 <p>UCP1 can transport protons through two different hypothesized mechanisms. In the first model, UCP1 transfers protons from intermembrane space to mitochondria matrix. Fatty acids provide essential free carboxy groups catalyzing proton (H+) translocation. In this model, Coenzyme Q(CoQ) serves as a necessary cofactor of UCP1, activating the protein functions.</p>

                 <p>In the second model, free fatty acids (FFAs) combine with protons with carboxy groups, then flipping across inner mitochondria membrane. After FFAs flipping to the matrix side, UCP1 removes protons from carboxy groups, flipping the anion form FFAs back to the innermembrane space. (fig.??)The anion form FFAs bind to protons again, transferring more protons into the matrix. </p>

                 <p>In the second model, free fatty acids (FFAs) combine with protons with carboxy groups, then flipping across inner mitochondria membrane. After FFAs flipping to the matrix side, UCP1 removes protons from carboxy groups, flipping the anion form FFAs back to the innermembrane space. (fig.??)The anion form FFAs bind to protons again, transferring more protons into the matrix. </p>

                 <div class="tip">(fig.??)</div>

                 <div class="tip">(fig.??)</div>

                 <p>Through these two div mechanisms, proton gradient on either side of inner membrane are formed. Generally, the oxidative phosphorylation of ADP into ATP takes place within the mitochondrial inner membrane respiratory chain. However, the coupling of mitochondrial respiration and ATP synthesis is not complete (Nicholls, 1974; Brand, 1977). Thus in several tissues there is a proton leak through the inner mitochondrial membrane that is not associated with ATP synthesis. And in these tissues, UCPs produce heat.

                 <p>Through these two div mechanisms, proton gradient on either side of inner membrane are formed. Generally, the oxidative phosphorylation of ADP into ATP takes place within the mitochondrial inner membrane respiratory chain. However, the coupling of mitochondrial respiration and ATP synthesis is not complete (Nicholls, 1974; Brand, 1977). Thus in several tissues there is a proton leak through the inner mitochondrial membrane that is not associated with ATP synthesis. And in these tissues, UCPs produce heat.

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