Note: you'll have already seen a question with the same image below. The question order shouldn't be randomised. There are a few questions with this same image.

The image below shows the titration curve for a dipeptide (think what that means).

The pI for this dipeptide is 5.0

What would the average charge of this dipeptide be at a pH of 8?

(You should be able to work this out even without knowing the precise identity of the amino acids.)

Note: you'll have already seen a question with the same image below. The question order shouldn't be randomised. There are a few questions with this same image.

The image below shows the titration curve for a dipeptide (think what that means).

The pI for this dipeptide is 5.0

What would the average charge of this dipeptide be at a pH of 1?

(You should be able to work this out even without knowing the precise identity of the amino acids.)

Shown below is a titration curve for a dipeptide. (Think about what this means...)

The number of ionisable groups in this dipeptide is:

Note: you'll have already seen a question with the same image below. The question order shouldn't be randomised. There are a few questions with this same image.

The image below shows the titration curve for a dipeptide (think what that means).

The pI for this dipeptide is 5.0

What would the average charge of this dipeptide be at a pH of 1?

(You should be able to work this out even without knowing the precise identity of the amino acids.)

Shown below is a titration curve for a dipeptide. (Think about what this means...)

The number of ionisable groups in this dipeptide is:

Which is more stable?

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?

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.

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.

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?