Final answer:
Signal peptide patterns (SPPs) consist of N-terminal hydrophobic regions that guide proteins to their cellular destination. Signal anchors become integrated into the membrane, with stop-transfer sequences trapping the protein in the fatty acid interior of the membrane.
Step-by-step explanation:
The correct answer is: B) N-terminal hydrophobic regions; integration into the membrane. Signal peptide patterns (SPPs) typically consist of N-terminal hydrophobic regions. Signal peptides are short amino acid sequences at the N-terminus of proteins that guide their insertion into membranes, either the endoplasmic reticulum (ER) membrane in eukaryotes or the plasma membrane in prokaryotes. The hydrophobic nature of these sequences helps in membrane integration. As for the fate of signal anchors, they play a crucial role in membrane proteins. Signal anchors guide the insertion of proteins into membranes, and once integrated, they become transmembrane domains, stabilizing the protein within the lipid bilayer. This process is essential for the proper functioning of membrane proteins involved in diverse cellular functions.