BIO 320 Lecture Notes - Lecture 2: Integral Membrane Protein, Alpha Helix, Calnexin
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Sketch the structure of the srp and label its parts and their functions. (11) Methionine helps the srp to accommodate the alpha helix, so in the event of the mutation it would be too specific to accomodate all the hydrophobic stretches (accommodate a-helix with different r groups) Translational pause domain gives ribosome time to associate. Signal-sequence-binding pocket maixnly hydrophobic that must occur for the protein to be soluble in the er lumen? (12-16) Walk through/act out the steps of srp binding to the signal sequence. Discuss how post-translational translocation is more difficult. Design a single-pass integral membrane protein with an internal non-cleavable signal sequence. What does the protein look like from n-terminus c-terminus? (21) What is the role of time in protein degradation, and glucose trimming? (33-34) What might happen if mannosidase was removed from the cell? cytosol through erad pathway.
