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BIO 320 Lecture3slides_2009

BIO 320 Lecture3slides_2009 - Lecture 3 Protein Folding...

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1 Lecture 3 (01/27/09) Protein Folding, Degradation & Ubiquitin ***OPTIONAL READING: review articles*** Goldberg, Elledge & Harper. (2001) The Cellular Chamber of Doom. Scientific American 284 :68-73. Mukhopadhyay & Riezman. (2007) Proteasome-Independent Functions of Ubiquitin in Endocytosis and Signaling. Science 325:201-205 Sowa & Harper. (2006) From Loops to Chains: Unraveling the Mysteries of Polyubiquitin Chains Specificity and Processivity. ACS Chem. Biol. 1:20-24 Downloadable @ blackboard The folding of a protein is controlled by its amino acid sequence Alberts, 3-5 •Some proteins fold on their own •Most proteins need help to fold Few proteins can refold after complete denaturation. Alberts, 3-6 Most proteins begin to fold as they are synthesized Alberts, 6-84 Some proteins require the binding of cofactors or covalent modifications to fold into their mature conformation. Alberts, 6-82 Folding pathways for a protein Alberts, 6-85 Nascent proteins fold into an initial structure that then matures into the final conformation
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2 Monomeric Multimeric
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