Anatomy and Cell Biology 4429A Lecture : Protein Folding

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tanhippopotamus305

22 Dec 2011

School

Western University

Department

Anatomy and Cell Biology

Course

Anatomy and Cell Biology 4429A

Professor

Paul Walton

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Document Summary

Chaperones allow proteins to fold, 1/3 of the proteins that are folded do not fold properly and have to be disposed of. Hsp70 delivers proteins to the lysosomes or proteosomes if you are a misfolded proteins. A small fraction of proteins can fold on their own and some fold with the help of a molecular chaperone. Some proteins don"t do any of one of these three things pictured in the diagram and find themselves aggregated together in insoluble clumps. Cells are not very good at not very good at unfolding proteins. The pathway this protein is involved with will be rerouted to a different pathway or will stop. The protein could also do something new which might be toxic to the cell, or undergo a gain of function. Accumulation - if there is a mutation and this protein isn"t targeted to be destroyed, these proteins might accumulate.

Related Questions

Chaperone proteins typically recognize a number of different unfolded protein substrates. Similarly, there are certain in Unfoldases that recognize misfolded proteins and attempt to unfold them, in order to allow them to refold correctly. What might be a common mechanism by which Chaperones and Unfoldases recognize their different protein targets(in other words, what is mostlikely common to the proteins recognized by either Chaperones or Unfoldases)?

whitescorpion85

In cells, folding of the protein tau is typically assisted by chaperoneswhich themselves change shape during the folding of the targetedprotein. Describe how the shape changes in two different types of chaperones - Hsp70 and Hsp60 - are coupled to folding of newly synthesized tau and the role of ATP in this process. Improperly folded tau is targeted for destruction, but the native (properly folded) tau is not. Explain the reason for the different fates of these two versions of the tau polypeptide. Some folded forms of tau accumulate and cause serious neurological disease called âtauopathiesâ; what might account for this aberrant tau accumulation?

periwinkletiger90

1. How do viral proteins get localized to the nucleus?

2. How do viral proteins get localized to the plasma membrane?

3. How does a nascent protein get targeted to the ER?

4. What amino acid residue on a target protein is attached to the sugar?

5.Where in the cell are N-linked oligosaccharides FIRST added to a glycoprotein?

6.Where in the cell does the initial sugar get processed into its mature form?

7. That is, which exact compartment(s) of the secretory pathway is mannose removed? Galactose added? Sialic acid added? How does the position of glycosylation (N-linked vs internal) affect which chaperone is used to properly fold proteins in the ER?

8. What compartments comprise the secretory pathway in mammalian cells?

9.How do proteins get transported from the ER to the Golgi?

10.How do the transport vesicles return from the Golgi to the ER?

11.What happens to their components when they get there? How does poliovirus inhibit the secretory pathway?

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Anatomy and Cell Biology 4429A Lecture : Protein Folding

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