The image below shows part of a structure of a protein, with several amino acids highlighted in ball and stick representation.

Which one statement concerning this region of the structure is true?

Integral membrane proteins associate with the membrane through:

The graph below shows data for the fractional saturation of a protein with varying concentrations of ligand.

Using the graph and your knowledge of Kd, determine the concentration of ligand (in nM; nanomolar) required to achieve 1% of protein bound.

If Kd = 50 nM...

...what [L] is required for θ = 10%?

Kd = 200 nM.

If [L] = 20 μM, what is θ?

Which answer best represents the Kd that can be estimated from the below binding curve?

A hydropathy plot of the amino acid sequence of a membrane protein begins with a region of high negative hydrophathy, followed by three regions of high positive hydropathy, and ends with a region of high negative hydropathy. Each of the regions of high positive hydropathy spans around 25 residues. The first two regions of high positive hydropathy have a short region of negative hydropathy between them. The second two regions of high positive hydropathy have a far longer region of negative hydropathy between them.

Which (terribly sketched by Nathan) schematic below best fits with the description above?

An enzyme, E, displays negative cooperativity (allosteric behaviour) for its substrate, S, in the presence of a modulator, M.

Which curve below (A, or B) represents the dependence of the initial velocity of E on the concentration of S in the presence and absence of M.

In studying an enzyme reaction obeying Michaelis-Menten kinetics, experimental data were transformed and plotted as a double reciprocal plot. A trendline was fitted to the data and the equation of the straight line was found to be:

y = 0.1x + 0.006667

What are the values of V_max and K_m for this reaction?

An uncompetitive enzyme inhibitor: