A group of membrane proteins can be extracted from membranes only by using detergents. All the proteins in this group have a similar amino acid sequence at their C-terminus: -KKKKKXXC (where K stands for lysine, X stands for any amino acid, and C stands for cysteine). This sequence is essential for their attachment to the membrane. What is the most likely way in which the C-terminal sequence attaches these proteins to the membrane? The cysteine residue is covalently attached to a membrane lipid. The peptide spans the membrane as an α helix. The peptide spans the membrane as part of a β sheet. The positively charged lysine residues interact with an acidic integral membrane protein.

6) Proteins can be modified by phosphorylation, which adds a phosphate group to the hydroxyl group of serine, threonine, or tyrosine residues. The R-group for phosphoserine is shown at right. A) The image below is an Isoelectric focusing strip that shows the unphosphorylated protein-of-interest (in blue). To which side of the unphosphorylated protein would you expect to see the phosphorylated protein? (Draw an arrow to indicate direction). Briefly justify your answer. un-phosphorylatable: Low pH Justify: B) To study the effects of phosphorylation, researchers often mutate a Ser/Thr to appear as though it is always phosphorylated or never phosphorylated at a particular site. What amino acid substitution should you use to preserve similar dimensions as Ser (or Thr) but make the side chain appear to be: constitutively (always) phosphorylated: Justify: Ser or Thr → O O=P-O O I CH₂ Ser or Thr➜ Phosphoserine High pH

I’m not sure which answer is correct for this question can you please help?

Please use Transferrin receptor as an example of the protein whose pathway is being traced. If it is easier or possible, can there be a labeled drawing to explain.