Test 1 review session Bio 320

Test 1 review session Bio 320 - 9/21/09 Bio 320 20 M/C 10...

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9/21/09 Bio 320 20 M/C 10 fill in /short 3 essay type 1 longer 2 shorter 3 questions on the first lecture (no essays) Domains: regions of proteins that fold independently of each other A protein could have two domains Catalytic Regulatory Could use a protease to cut the domains apart When cut free the regulatory would be free to regulate and the catalytic domain can function as a separate entity Chaperones chapereonins Athensin cage Molecular chaperones bind directly to the protein and try to refold it Both involve the use of ATP If it doesn’t work you put ubiquiton on and take it to the proteasome Proteasome chops it up (in the cytoplasm) Trying to get hydrophobic regions into the inside so if there is a hydrophobic region on the outside that is one reason why something could be targeted The outer leaflet of the lipid raft: sphingolipids and cholesterol On the inside: phosphotidilinastitol (important in cell signaling) Lipid rafts seem to concentrate F10 ATPase A number of individual subunits form a ring and that ring is connected to a shaft. Protons drive it at the base
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This note was uploaded on 11/11/2009 for the course BIO Cell bio taught by Professor Poenie during the Spring '09 term at University of Texas at Austin.

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Test 1 review session Bio 320 - 9/21/09 Bio 320 20 M/C 10...

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