bis_104_pq_21_ans_fall_07 - size alpha globin protein, not...

Info iconThis preview shows page 1. Sign up to view the full content.

View Full Document Right Arrow Icon
BIS 104 Practice Question #21 21. a) Give a one or two sentence description of the signal peptide hypothesis. Secretory proteins contain a signal sequence at their N-terminus that directs the emerging polypeptide and ribosome to the ER membrane. The polypeptide is then moved into the cisternal space of the ER through a protein-lined aqueous channel in the ER membrane. b) Describe the results you would expect to observe if you added mRNA coding for alpha globin to a cell-free translation system in (1) the presence, or (2) in the absence of added microsomes. (1) presence of microsomes: Since the mRNA has no signal sequence code, the translation system would synthesize native
Background image of page 1
This is the end of the preview. Sign up to access the rest of the document.

Unformatted text preview: size alpha globin protein, not associated with the microsomes. Therefore, a single protein band on SDS gel, that would be digestible by protease. (2) absence of microsomes: Same as above; only native alpha globin protein is made. (In describing your results remember that the protein products from the cell-free system are analyzed by SDS-PAGE). c) Why is the procedure described in (b) above an important control for the in vitro experiments described by Lingappa? It demonstrates that native alpha globin protein, in the absence of a signal sequence, does not associate non-specifically with an in vitro preparation of microsomes....
View Full Document

This note was uploaded on 08/18/2008 for the course BIS 104 taught by Professor Scholey during the Summer '08 term at UC Davis.

Ask a homework question - tutors are online