Shown below is a schematic diagram representing the primary structure of an integral membrane protein that traverses a cell membrane 4 times.

"N" and "C" represent the N- and C-termini of the protein.

Hydrophobic (red) and polar (blue) regions are colour coded.

When intact cells containing this protein in the membrane are treated with a chemical labelling reagent, the reagent reacts with lysine residues at the positions indicated by arrows.

Which regions of this protein are expected to protrude on the cytoplasmic side of the membrane?

Shown below is a cartoon of a polytopic membrane protein of known sequence and topology.

If you were to carry out a glycoproteomics experiment to analyse for the presence and position of glycosylation on this protein, out of the options below which do you think would be the most likely result?

Shown below is a cartoon of a polytopic membrane protein of known sequence and topology.

If you were to carry out a glycoproteomics experiment to analyse for the presence and position of glycosylation on this protein, out of the options below which do you think would be the most likely result?

Shown below is a region of a protein containing a single transmembrane helix.

The position and hydrophobicity of each amino acid is shown.

What is the estimated position of the transmembrane domain?

Shown below is a cartoon of a polytopic membrane protein of known sequence and topology.

If you were to carry out a glycoproteomics experiment to analyse for the presence and position of glycosylation on this protein, out of the options below which do you think would be the most likely result?

Shown below is a region of a protein containing two transmembrane helices.

The position and hydrophobicity of each amino acid is shown.

What is the estimated position of the first transmembrane domain?

Shown below is a cartoon of a polytopic membrane protein of known sequence and topology.

If you were to carry out a glycoproteomics experiment to analyse for the presence and position of glycosylation on this protein, out of the options below which do you think would be the most likely result?

Shown below is a region of a protein containing a single transmembrane helix.

The position and hydrophobicity of each amino acid is shown.

What is the estimated position of the transmembrane domain?

Shown below is a region of a protein containing two transmembrane helices.

The position and hydrophobicity of each amino acid is shown.

What is the estimated position of the second transmembrane domain?

Shown below (left) is a schematic diagram representing the conformational equilibrium of a heteromeric allosteric enzyme. Note that the R state has higher catalytic activity than the T state.

Also shown below (right) are the kinetics curves for this enzyme alone and in the presence of an allosteric modulator.

Based on the kinetics curves, which site on the enzyme (A-D) is this modulator likely to bind to most strongly?