Question 1

Which of the following statements best describes a zwitterion form of an amino acid at neutral pH?

Accepted Answer

The amino group is protonated and the carboxyl group is deprotonated.

Question 2

Which equation is used to calculate the pH at the isoelectric point ($$pI) of a $$simple amino acid with two ionizable groups?

Accepted Answer

$$pI = \frac{pK_{a1} + pK_{a2}}{2}$$

Question 3

Which amino acid is most likely to absorb ultraviolet light at 280 nm due to its aromatic side chain?

Accepted Answer

Tryptophan

Question 4

A patient with Kwashiorkor is most likely deficient in which class of amino acids?

Accepted Answer

Essential amino acids

Question 5

Which of the following best explains why the trans configuration of a peptide bond is more stable than the cis configuration?

Accepted Answer

Trans configuration reduces steric interference between side chains.

Question 6

Which amino acid is most likely to form disulfide bonds, contributing to protein tertiary structure?

Accepted Answer

Cysteine

Question 7

Which of the following is a correct application of the Henderson-Hasselbalch equation for an amino acid titration curve?

Accepted Answer

$$pH = pK_a + \log \left( \frac{[A^-]}{[HA]} \right)$$

Question 8

Which secondary structure is characterized by hydrogen bonds between adjacent polypeptide chains and is stabilized by frequent alanine and glycine residues?

Accepted Answer

β-pleated sheet

Question 9

What is the main biological significance of the quaternary structure in proteins such as hemoglobin?

Accepted Answer

It enables complex interactions for regulation and allosteric behavior.

Question 10

Which of the following is a correct description of an enzyme's active site?

Accepted Answer

It is the region where substrate molecules bind and undergo a chemical reaction.

Question 11

Which of the following best describes the induced fit model of enzyme-substrate interaction?

Accepted Answer

The enzyme changes shape to better accommodate the substrate upon binding.

Question 12

Which class of enzymes catalyzes the transfer of functional groups from one molecule to another?

Accepted Answer

Transferases

Question 13

What is the effect of a competitive inhibitor on the Michaelis-Menten kinetic parameters?

Accepted Answer

It does not change $$V_{max}$$ but increases $$K_m.$$

Question 14

Which vitamin is water-soluble, acts as a cofactor for many enzymes, and is not stored in the body?

Accepted Answer

Vitamin C

Question 15

Which of the following is true regarding the activation energy ($$E_a) in $$enzyme-catalyzed reactions?

Accepted Answer

Enzymes decrease the activation energy, increasing the reaction rate.

Question 16

Which of the following amino acids is most likely to be found in the interior of a globular protein due to its nonpolar side chain?

Accepted Answer

Leucine

Question 17

Which structural level of a protein is defined by the tridimensional arrangement of all atoms in space, including interactions such as hydrogen bonds, non-polar interactions, and disulfide bonds?

Accepted Answer

Tertiary structure

Question 18

Which of the following is a correct representation of the Michaelis-Menten equation for enzyme kinetics?

Accepted Answer

$$v = \frac{V_{max}[S]}{K_m + [S]}$$

Question 19

Which of the following statements about peptide bonds is correct?

Accepted Answer

Peptide bonds are planar due to resonance stabilization.

Amino Acids, Peptides, Proteins, and Enzymes: Structured Study Notes

Guida di studio - Domande di pratica

Study guide - Flashcard