BSC 300 Study Guide - Midterm Guide: Nuclear Pore, Gtpase, Prophase

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Synthesis of secreted proteins, integral plasma-membrane proteins, and proteins destined for the. In cotranslational translocation, the signal recognition particle (srp) first recognizes and binds the. In addition, the channel is gated so that it is open only when a polypeptide is being translocated. In post-translational translocation, a completed secretory protein is targeted to the er membrane by interaction of the signal sequence with the translocon: the polypeptide chain is then pulled into the er by a ratcheting mechanism that requires. Atp hydrolysis by the chaperone bip, which stabilizes the entering polypeptide. In bacteria, the driving force for post-translational translocation comes from seca, a cytosolic atpase that pushes polypeptides through the translocon channel. Single-pass membrane proteins contain one or two topogenic sequences. In multipass membrane proteins, each -helical segment can function as an internal topogenic sequence, depending on its location in the polypeptide chain and the presence of adjacent positively charged residues.

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