Protein Synthesis

Question 1

(Blank) RNA is the type of RNA that serves as a transcript of the DNA code for protein synthesis.

Answer 1

Messenger

Question 2

(Hydrophobic/Hydrophilic) amino acids including, serine, threonine, asparagine, and glutamine are capable of forming hydrogen bonds with their side-chains.

Answer 2

Hydrophilic

Question 3

During the elongation phase of mRNA translation, a new aminoacyl-tRNA will recognize a complementary codon at the site of a ribosome.

Answer 3

A-Site

Question 4

Alanine, valine, leucine, methionine, isoleucine and glycine are all (polar/nonpolar) amino acids.

Answer 4

non-polar

Question 5

(Amino acid) can be converted to α-ketoglutarate, an intermediate of the Krebs cycle.

Answer 5

Glutamate

Question 6

(Hydrophilic/Hydrophobic) amino acids are more likely to face the aqueous environment rather than the protein interior.

Answer 6

Hydrophobic

Question 7

synthetase is the enzyme that uses ATP to load a specific amino acid onto the tRNA molecule.

Answer 7

Aminoacyl-tRNA synthetase

Question 8

(Exons/Introns) are repetitive, interspersed segments of DNA that do not code for amino acid sequences.

Answer 8

Introns

Question 9

On the Michaelis Menten graph, represent the state when all the active sites on all of the enzyme become saturated.

Answer 9

Meximum Velocity or Vmax

Question 10

RNA differs from DNA in that it has the nitrogenous base instead of thymine.

Answer 10

Uracil

Question 11

A protein’s primary structure is .

Answer 11

Its linear sequence of amino acids

Question 12

After a peptide bond is formed between the amino acids, the tRNA molecule will from the A site to the P site.

Answer 12

translocate or move

Question 13

In translation, the empty tRNA molecule will translocate from the P site to the site, where it is then released.

Answer 13

E-site

Question 14

(Exons/Introns) are the sequences of genes that code for specific amino acid sequences.

Answer 14

Exons

Question 15

At physiologic pH, the carboxyl group in the amino acid is likely to be (protonated/deprotonated) and the amino group is likely to be protonated.

Answer 15

deprotonated

Question 16

α-helix and β-pleated sheets are examples of structures.

Answer 16

secondary

Question 17

The reductive amination of pyruvate produces (amino acid) .

Answer 17

alanine

Question 18

Tyrosine, tryptophan, and phenylalanine all contain an (aliphatic/aromatic)

Answer 18

aromatic

Question 19

Arginine is considered a(n) (acidic/basic) amino acid.

Answer 19

basic

Question 20

The formation of a peptide bond is a (hydrolysis/condensation) reaction.

Answer 20

condensation

Question 21

Inactive hydrophobic amino acids such as glycine, alanine, valine, leucine and isoleucine are more likely to be found in the protein (interior/exterior)

Answer 21

interior

Question 22

The (acetylation/transamination) of certain amino acids provide precursor molecules for metabolic pathways.

Answer 22

transamination

Question 23

Leucine and lysine are the only two solely (ketogenic/glucogenic) amino acids.

Answer 23

ketogenic

Question 24

Some proteins may contain a short peptide called the sequence, allowing it to bind to the membrane of the rough endoplasmic reticulum.

Answer 24

signal

Question 25

is an essential amino acid that has a positively charged imidazole functional group.

Answer 25

Histidine

Question 26

Protein release factors add water to the bond between the polypeptide and the tRNA at the P site.

Answer 26

hydrolyze

Question 27

On the Michaelis Menten graph, is the concentration of substrate at which the speed of the reaction is exactly half the maximum velocity.

Answer 27

Km

Question 28

is the only achiral amino acid.

Answer 28

Glycine

Question 29

RNA is the type of RNA that serves as the location of protein synthesis during DNA translation.

Answer 29

Ribosomal

Question 30

Only (L/D) -forms of amino acids are used by cells.

Answer 30

L-form

Question 31

RNA is the type of RNA that recognizes the mRNA transcript and brings the specified amino acids.

Answer 31

Transfer

Question 32

structure is the overall shape of the polypeptide chain.

Answer 32

Tertiary

Question 33

An amino acid that has both positive and negative charges but has a net charge of zero is also known as a .

Answer 33

zwitterion

Question 34

The initiator tRNA can begin mRNA translation when it encounters the start codon triplet .

Answer 34

AUG

Question 35

Proteins are made of (L/D) -amino acids.

Answer 35

L-amino acids

Question 36

means that the same amino acid can exist in two forms that are mirror images of each other.

Answer 36

Chirality

Question 37

In the process of translation, bring specific amino acids to the ribosome that are complementary to the corresponding mRNA triplet codon.

Answer 37

tRNAs

Question 38

A reaction spontaneously occurs when the is negative.

Answer 38

Gibbs free energy, or ΔG

Question 39

Aspartic acid and glutamic acid become (positively/negatively) charged with the loss of a proton in a neutral solution.

Answer 39

negatively

Question 40

To terminate mRNA translation, a must bind to the stop codon at the A site.

Answer 40

Protein Release Factor

Question 41

Enzymes (can/can’t) be reused.

Answer 41

can

Question 42

Enzymes function by decreasing the by stabilizing the transition state.

Answer 42

activation energy - or ΔG‡

Question 43

A low Km means the enzyme has a (high/low) affinity for its substrate.

Answer 43

high

Question 44

structure involves multiple polypeptide chains forming a larger protein structure.

Answer 44

Quaternary

Question 45

A is a section of a DNA molecule that carries the order of one specific polypeptide chain.

Answer 45

gene

Question 46

The two amino acids that contain a sulfur molecule are cysteine and .

Answer 46

methionine

Question 47

Enzymes act as catalysts which at which biochemical reactions happen.

Answer 47

speed up the rate

Question 48

is a unique amino acid in which the R group is also bound to the amino group, forming a ring structure that causes structural kinks in polypeptide chains.

Answer 48

Proline