L2-Protein Folding, Degradation, & Ubiquitin

L2-Protein Folding, Degradation, & Ubiquitin - Lecture...

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Lecture 2 Protein Folding, Degradation ***OPTIONAL READING: review article*** Goldberg, Elledge & Harper. (2001) The Cellular Chamber of Doom. Scientific American 284 :68-73.
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The folding of a protein is controlled by its amino acid sequence QuickTime™ and a Animation decompressor are needed to see this picture. Some proteins fold on their own Most proteins need help to fold Alberts, 3-5
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Few proteins can refold after complete denaturation. Alberts, 3-6
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Most proteins begin to fold as they are synthesized Alberts, 6-84
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Monomeric Multimeric HSP-60 HSP-70 Heat Shock Proteins = proteins involved in the folding of new proteins or refolding of proteins that started to unfold after heat treatment. Two Types of Chaperones
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Folding of Proteins by HSP-70 HSP-70 uses ATP to fold proteins Many monomers bind along the length of the protein Can bind as soon as protein is out of the ribosome Can also Unfold a partially misfolded protein Useful to maintain a protein in an extended conformation Alberts, 6-86
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L2-Protein Folding, Degradation, & Ubiquitin - Lecture...

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