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SC BIOL 302 - Proteins

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BIOL 302 1st Edition Lecture 6Outline of Previous Lecture I. Macromoleculesa. Protein Structuresb. Protein DomainOutline of Current LectureI. Proteinsa. Quaternary structuresb. Self-assemblyc. AllosteryCurrent LectureI. Quaternary Structuresa. Most proteins have multiple activitiesb. DNA polymerase needs to bind to DNA i. Important for Dimerization and activating the gene expression from a specific domainc. Proteins have a module structure which functions structures as seperabled. Most proteins have multiple subunits e. But they come together by self assembleII. Self-Assemblya. Complicated structures have series of R groups that match with another R group to make bonds i. All come from DNAb. They self assemble spontaneouslyi. Eg: Tobacco Mosaic Virus1. Purifies RNA then add in a test tube, it will assemble spontaneously and comes together to make the virusii. Eg2: Bacterial Ribosome1. Can’t throw everything in test tube, has to be added one by one inthe right order, each protein is encoded by a different gene. c. Abnormal Self Assemble:i. Reasons for many diseasesii. Beta ambaloid – kill the nerve cells in the brainThese notes represent a detailed interpretation of the professor’s lecture. GradeBuddy is best used as a supplement to your own notes, not as a substitute.1. Many infect the brain and loose liver cellsiii. A lot of diseases are centered to the brain. Cell death releases toxinsiv. Proin Disease 1. Infectious disease to the brain (Alzheimer’s): Examples:a. Kuru (in Humans): discovered in Africa. Very high incedius of brain damages. Thought it was genetic at first, but figured out it was infectious. More in woman, the origin of the disease was discovered through the cannibalism of the dead (uncooked). Ingesting this was infectious to the prion disease (no nucleic acid)b. Scrapie (sheep): genetic dispositionc. Bouine (Mad Cow Disease): FDA watching out cows that couldn’t get up properly and was sick (Ireland, England, France outbreak and covered it up). Over 450 thousands ofsickness went into the meat (1980s-1990s)d. Crutzfelot (Jacob’s Disease): Just like Mad Cow’s Disease but in humans instead of cows. Due to eating the infected meat.i. To prevent they checked on the animals and did a lot of testing2. Pure proteins (pN) is what everyone synthesizes for the brain which doesn’t self assemble and transfers copper3. Infected proteins (pI): have the same amino acids but they self assemble and forms large sequences (254 aa). Can have the same sequence but have to be modernized. Function – aggregates, which kill the brain. III. Allosterya. Allosteric transition: can undergo induced chain and go through major changesi. Binds to other moleculesii. Major changes in functionb. Can be switched on/offc. Can have a molecule that would bind to a protein i. Changes the shape by causing the tryon to moved. Inactive/active e. P53 can be modified to take out 3 or 4 activities f. Movements:i. Parts can be induced to move – work can be done through a pumpg. Motor Proteins: (don’t need to memorize any but the last one)i. Kinesin – 4 proteins 1. Moves organelles around the cell by binding to microtubules2. 2 Heavy Chains (1,200 aa) that forms a coil that colds it together like cargo3. 2 Light Chains (600 aa) which is responsible to binding to the mitochondria4. Travels along in microtubules carrying “stuff”5. Movement: microtublina. Binds through motors domain (ATP bind- allosteric conformation chain where it loses a it’s leg)b. ATP gets hybridize to ADP +Pc. *Rebinds to the other leg, second leg steps downd. Lastly, it releases ADP, upper leg bings to the tubulin6. It was first thought that everything happen through


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SC BIOL 302 - Proteins

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