Question

1.The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics:

2/27/ 20

V0 (mol/min)

   217
   325
   433
   488
   647

Substrate added (mmol/L)

0.8 2 4 6 1,000

      

The Km for
A) 1 mM., B) 1000mM, C) 2mM, D ) 4mM, E) 6mM

this enzyme is approximately:

2. To

1. A) the enzyme concentration.

2. B) the initial velocity of the catalyzed reaction at [S] >> Km.

3. C) the initial velocity of the catalyzed reaction at low [S].

4. D) the Km for the substrate.

5. E) both the enzyme concentration and the initial velocity of the catalyzed reaction at

   [S] >> Km.

3. An enzyme that can convert glucose into fructose is a member of which class of enzymes?

A) Oxidoreductases, B)Transferase, C) Hydrolases, D) Lyases, E) Isomerases

4. Which amino acid is NOT capable using its side chain (R group) to participate in general acid-base catalysis?
A) Asp, B) His, C) Ser, D) Val, E) Lys

calculate the turnover number of an enzyme, you need to know:

5. Treatment of methanol poisoning by using ethanol is an example of what type of enzyme inhibition?
A) mixed inhibition, B) uncompetitive inhibition

C) noncompetitive inhibition D) Competitive inhibition, E) Suicide Inhibition

6. What functional groups are present on this molecule?

A) ether and aldehyde, B) Hydroxyl and Aldehyde, C) Hydroxyl and Carboxylic acid, D) hydroxyl and Ester , E) hydroxyl and ketone

7. Which statement about intrinsically disordered proteins is TRUE?

A) B) C)

D) E)

They contain small hydrophobic cores.
They represent misfolded conformations of cellular proteins.
They have no stable three-dimensional structure and therefore have no cellular function.
They are responsible for proteostasis.
They can interact with multiple protein-binding partners and are central to protein interaction networks.

8.
protein aggregate?

Which disease is NOT one characterized by or associated with an unfolded

A) Alzheimer disease, B) Diabetes, C) Parkinson Disuease
D) Scurvy, E) All of these diseases are linked to unfolded protein aggregates

9. Which amino acid when repeated six to ten times at the N- or C-terminal ends of a protein allows that protein to bind to Ni2+ ions?

a.Glu, b. His, c. Ala, d. Tyr, e. Asp

10. The biochemical activity of a protein, such as its enzymatic activity, is called its _____ function.

a. phenotypic , b. genotypic, c. cellular, d. molecular, e. organismal

Answer 1

10. The biochemical activity of a protein, such as its  enzymatic activity is called its molecular function. Because proteins as biologically known as catalyst. So enzymes are also act as catalyst which upon the molecular reactions.

9. The amino acid when repeated six to ten times, at N or C terminals ends of proteins allows that protein to bind to Ni2+ ions is his. because, the presence of two different residues called his and cys are help in the binding of peptide bond with transition metal ions. peptides form an link with the disulfide bridges.

8. Scurvy is the disease which are not related with the unfolded protein aggreates,  type 2 diabeaties are caused by unfolded protein aggreates. Alzeheimer and parkinson are caused by unfoled protein aggreates.

7. The statements A,B C, D are true about intrinsically disordered proteins(IDP).  

5.Treatment of methanol poisoning by using ethanol is an example of competitive inhibition.