logo

Crowdly

BCH2011 - Structure and function of cellular biomolecules - S1 2025

Looking for BCH2011 - Structure and function of cellular biomolecules - S1 2025 test answers and solutions? Browse our comprehensive collection of verified answers for BCH2011 - Structure and function of cellular biomolecules - S1 2025 at learning.monash.edu.

Get instant access to accurate answers and detailed explanations for your course questions. Our community-driven platform helps students succeed!

When added to a solution at an enzyme concentration of 0.1 μM, chymotrypsin catalyses the hydrolysis of a peptide substrate with the following Vmax and Km values.

  • Vmax = 300 μM s-1
  • Km = 3 mM

If the same reaction is repeated but using a chymotrypsin concentration of 0.2 μM, what will be the values of Vmax, Km, and kcat under these new conditions?

0%
0%
100%
0%
View this question

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.

Image failed to load

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

0%
0%
100%
0%
View this question

Shown below is a free energy diagram representing a generic reaction of a substrate (S) to give a product (P), in the absence and presence of an enzyme.

Specific points on the free energy diagram are labelled A-D.

Free energy differences are labelled by arrows 1-14 on the right with the following colour code:

  • Black: Transitions between S and P
  • Red: Other transitions to/from S
  • Cyan: Other transitions to/from P

[Note that a free energy difference is defined as the free energy of the destination (arrow head) minus the free energy of the origin (arrow tail)].

Image failed to load

Which point represents the transition state of the enzyme-catalysed reaction?

0%
100%
0%
0%
View this question

Shown below is a table listing the initial rate of an enzyme-catalysed reaction at various substrate concentrations.

The enzyme concentration used was 100 nM (0.1 μM).

Image failed to load

What is the Km value for this reaction?

Type your answer as a number in the same units listed in the table.

Do not type the units or any other additional characters.

View this question

Shown below is the Lineweaver-Burk (double reciprocal) plot for an enzyme-catalysed reaction carried out in the presence of three different concentrations of the same inhibitor.

Image failed to load

Which of the following statements regarding the interactions of this inhibitor is most likely to be correct?

0%
0%
0%
100%
View this question

Shown below is a table listing the initial rate of an enzyme-catalysed reaction at various substrate concentrations.

The enzyme concentration used was 100 nM (0.1 μM).

Image failed to load

What is the kcat value for this reaction?

Type your answer as a number in units of min-1.

Do not type the units or any other additional characters.

View this question

One strategy used by enzymes to catalyse biochemical reactions is described below.

Amino acid side chains in the active site of an enzyme can protonate or deprotonate functional groups on the substrate, thus providing a pathway to the product that does not readily occur in the absence of the enzyme.

This catalysis strategy is called:

0%
0%
0%
100%
View this question

Select the term that best fits in the blank space to make the following statement correct.

By facilitating the conversion of one molecule to another many times repeatedly, an enzyme exhibits the property of _______________ .

100%
0%
0%
0%
View this question

The graph below displays a set of kinetics data for an enzyme that follows Michaelis-Menten kinetics.

Image failed to load

Estimate the Vmax value (in units of μM/s) for this data set.

 

Note: You should type the number only (not the units or any other characters).

View this question

The graph below displays a set of kinetics data for an enzyme that follows Michaelis-Menten kinetics.

Image failed to load

Estimate the Km value (in units of mM) for this data set.

 

Note: You should type the number only (not the units or any other characters).

View this question

Want instant access to all verified answers on learning.monash.edu?

Get Unlimited Answers To Exam Questions - Install Crowdly Extension Now!