questions - Review questions for lecture 33 33.1 What makes...

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Review questions for lecture 33 33.1) What makes the rough ER look different from the smooth ER in the electron microscope, and where is this distinguishing feature observed: in the ER lumen or on the cytoplasmic side of the ER. 33.2) Where is the site of phospholipid synthesis in a cell? 33.3) What are the roles of each of the following proteins during co-translational transport: SRP, SRP receptor, signal sequence, protein translocator, signal peptidase. 33.4) What would you predict to be the minimal length a polypeptide must be to be co-translationally transported into the ER. 33.5) Where is translation of a secreted protein initiated in the cell? 33.6) Why are secreted proteins at least 2200 daltons smaller than one would predict based on the sequence of the genes encoding these proteins? (hint: the average molecular weight of an amino acid is 110 daltons.) 33.7) Fig. 12-50 shows a schematic of a multipass transmembrane protein. The orientation of the polypeptide chain in the membrane is dictated by the orientation of the first start transfer sequence. Which side of the membrane would the C-terminus of the protein be on if you switched the negative and positively charged amino acids flanking the first start transfer sequence and deleted the hydrophobic domain corresponding to the first stop transfer sequence closest to the N terminus in the figure? 33.8) During the cotranslational transport process, start transfer and stop transfer sequences control the incorporation of transmembrane domains into the ER membrane. Only one of these two sequences interacts with SRP and the protein translocator. Which one interacts with SRP and the protein translocator. 33.9) Does the amino acid sequence of stop transfer sequence distinguish it from a start transfer sequence?
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Review questions for lecture 34. 34.1) How do BiP and protein disulfide isomerase contribute to the final state of a protein? Where are these proteins located in the cell and how can they impact on a protein that ends up on the outside of the cell? 34.2) What is meant by the term "N-linked glycosylation" and where does this occur? How does this differ from "O-linked glycosylation"? 34.3) Why is a phospholipid translocator required in the membrane of the ER? 34.4) GPI is an example of what type of molecule? What role does it play in generating an intergral membrane protein? 34.5) A protein in the lumen of the ER ends up on which side of the golgi membrane and on which side of the plasma membrane? 34.6) Vesicular transport can be divided into three phases: 1) Formation of the vesicle with the correct cargo, 2) Targeting the vesicle to the correct destination, 3) Fusion of the vesicle with the target membrane. Describe how the following proteins contribute to these phases of vesicular transport: Adaptin, Clathrin, Dynamin, COP, Sar1, v-SNARE, t-SNARE.
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