Sandbox Reserved 508: Difference between revisions

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Bottom row: ROS in a myocytes exposed to an adenovirus producing the UCP2 protein. DCF fluorescence is barely visible, representing little to no ROS presence.
Bottom row: ROS in a myocytes exposed to an adenovirus producing the UCP2 protein. DCF fluorescence is barely visible, representing little to no ROS presence.
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B. Quantitative representation of the changes in ROS levels corresponding to the fluorescence images in A using time-lapse confocal microscopy. The presence of UCP2 greatly reduces ROS levels, limiting damage to cardiac ventricular myocytes.
B. Quantitative representation of the changes in ROS levels corresponding to the fluorescence images in A using time-lapse confocal microscopy. The presence of UCP2 greatly reduces ROS levels, limiting damage to cardiac ventricular myocytes.
== Figures ==
== Figures ==
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through the membrane by UCP2.]]
through the membrane by UCP2.]]


<StructureSection load='2lck_pdb' scene='Sandbox_Reserved_508/2lck_pdb/10' size='500' side='right' caption='Structure of UCP 2 displaying key features. In this model of UCP2, the light sea green parts represent the alpha helices which are thought to be involved in the transport of protons. All negatively-charged amino acids, glutamic and aspartic, are colored crimson. These may be involved in the direct transport of protons through UCP2. All positively charged amino acids, except for Lys141 and Arg185, are colored navy. These may be involved in the transport of deprotonated fatty acid molecules through UCP2, as well. Lys141 and Arg185, which are speculated to bind to the UCP2 inhibitor, GDP, are colored light sky blue. Helix sequences, conserved between different UCP proteins, which may also have a role in fatty acid transport, are colored orange. Helices found in the matrix or the inter-membrane space are colored light aquamarine. Loops, which are not involved in the active site, are colored white.  '>
<StructureSection load='2lck_pdb' scene='Sandbox_Reserved_508/2lck_pdb/12' size='750' side='middle' caption='Structure of UCP 2 displaying key features. In this model of UCP2, the light sea green parts represent the alpha helices which are thought to be involved in the transport of protons. All negatively-charged amino acids, glutamic and aspartic, are colored crimson. These may be involved in the direct transport of protons through UCP2. All positively charged amino acids, except for Lys141 and Arg185, are colored navy. These may be involved in the transport of deprotonated fatty acid molecules through UCP2, as well. Lys141 and Arg185, which are speculated to bind to the UCP2 inhibitor, GDP, are colored light sky blue. Helix sequences, conserved between different UCP proteins, which may also have a role in fatty acid transport, are colored orange. Helices found in the matrix or the inter-membrane space are colored light aquamarine. Loops, which are not involved in the active site, are colored white.  '>




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