Biology 311C Lecture 7

Biology 311C Lecture 7 - September 9 2011 Biology 311C...

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September 9, 2011 Biology 311C Lecture 7 It is hard to predict a protein’s structure from its primary structure. Chaperonins are protein molecules that assist the proper folding of other proteins. Diseases such as Alzheimer’s Parkinson’s, and mad cow disease are the causes of an incorrectly folded protein. What happens when a protein folding in a cell is that the cap of the chaperonin attaches, causing the cylinder to change shape in such a way that it creates a hydrophilic environment for the folding of the polypeptide. Proteins function as hormones, antibodies, structure, etc. They need to be folded correctly in order to work. When a protein is denatures, it goes from active to inactive. Secondary and tertiary structures are lost when denatured. It is then recycled. The movement of a protein can be guided through the rails of our body. A protein might be carried to a chaperonin when it needs to be folded.
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This note was uploaded on 02/21/2012 for the course BIO 311 C taught by Professor Mcclelland during the Fall '09 term at University of Texas.

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Biology 311C Lecture 7 - September 9 2011 Biology 311C...

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