Quiz Questions

0.0(0)
studied byStudied by 0 people
0.0(0)
call with kaiCall with Kai
learnLearn
examPractice Test
spaced repetitionSpaced Repetition
heart puzzleMatch
flashcardsFlashcards
GameKnowt Play
Card Sorting

1/19

flashcard set

Earn XP

Last updated 7:44 PM on 1/30/26
Name
Mastery
Learn
Test
Matching
Spaced
Call with Kai

No analytics yet

Send a link to your students to track their progress

20 Terms

1
New cards

Matter is made of elements, which are composed of atoms

Which statement best describes the relationship between matter, atoms, and elements?
a.) Matter is made of elements, which are composed of atoms

b.) Atoms are made of elements, which are composed of matter
c.) Elements are made of matter, which are composed of atoms

d.) Matter is made of atoms, and atoms are composed of multiple elements

2
New cards

Ionic bond; water’s polarity separates the ions

What type of bond holds Na⁺ and Cl⁻ together in table salt, and how does water disrupt it?
a.) Covalent bond; water competes for shared electrons
b.) Ionic bond; water’s polarity separates the ions
c.) Hydrogen bond; water breaks hydrogen interactions

d.) Nonpolar bond; water dissolves all nonpolar molecules

3
New cards

Saturated fatty acids contain the maximum number of hydrogens, while unsaturated contain fewer due to double bonds.

Which of the following best describes the difference between a saturated and an unsaturated fatty acid?
a.) Saturated fatty acids contain only double bonds, while unsaturated contain none
b.) Saturated fatty acids are bent, while unsaturated are straight
c.) Saturated fatty acids contain the maximum number of hydrogens, while unsaturated contain fewer due to double bonds.
d.) Saturated fatty acids are amphipathic, while unsaturated are not

4
New cards

A water molecule is removed to form a covalent bond

Dehydration synthesis is used in forming both disaccharides and peptide bonds. What is common about the chemistry in both cases?
a.) A water molecule is added to link monomers
b.) A water molecule is removed to form a covalent bond
c.) Hydrogen bonds hold the monomers together
d.) Ionic interactions stabilize the new bond

5
New cards

They stabilize α-helices and β-sheets in proteins and base-pairing in DNA

How do hydrogen bonds contribute to the structure of both proteins and DNA?
a.) They hold amino acids together in primary protein structure and link nucleotides in RNA

b.) They stabilize α-helices and β-sheets in proteins and base-pairing in DNA
c.) They form peptide bonds in proteins and phosphodiester bonds in DNA
d.) They make proteins hydrophobic and DNA hydrophilic

6
New cards

Disulfide bonds

Which of the following is an example of a covalent bond between different amino acids of a protein?
a.) Hydrogen bonds
b.) Van der Waals
c.) Electrostatic
d.) Disulfide bonds

7
New cards

R group

Which of the following groups varies among different amino acids?
a.) hydrogen atom
b.) carboxyl group
c.) R group
d.) amino group

8
New cards

Peptide bonds

Which of the following bonds are not involved in tertiary structure?
a.) Peptide bonds

b.) Ionic bonds
c.) Hydrophobic interactions
d.) Hydrogen bonds.

9
New cards

Prions are misfolded proteins rich in β-pleated sheets that induce normal cellular PrP to refold into the diseased form

Which of the following best describes the mechanism by which prions cause disease?

a.) Prions contain nucleic acids that integrate into the host genome, altering protein expression
b.) Prions are misfolded proteins rich in β-pleated sheets that induce normal cellular PrP to refold into the diseased form
c.) Prions are bacterial pathogens that secrete toxins causing neuronal death
d.) Prions are viral particles that replicate within neurons using host enzymes

10
New cards

They exist as flexible chains in their functional state and often gain structure upon binding to partners

Which statement correctly describes Intrinsically Disordered Proteins (IDPs)?

a.) They have a stable, well-defined 3D structure in their functional state

b.) They exist as flexible chains in their functional state and often gain structure upon binding to partners

c.) They are always non-functional due to lack of stable structure

d.) They are misfolded proteins that cause disease, like prions

11
New cards

Protect chromosome ends

What is the primary role of telomeres?

a.) Protect chromosome ends

b.) Attach spindle fibers

c.) Bind histones

d.) Initiate transcription

12
New cards

It prevents excess product accumulation

How does feedback inhibition benefit a metabolic pathway?

a.) It increases ATP consumption

b.) It prevents excess product accumulation

c.) It permanently inactivates enzymes

d.) It increases enzyme diversity

13
New cards

A regulatory molecule induces a shape change away from the active site

Which scenario best explains allosteric regulation?

a.) A regulatory molecule induces a shape change away from the active site

b.) A substrate forms a covalent bond

c.) An enzyme is degraded

d.) A ligand binds the active site directly

14
New cards

DNA is more accessible

Why does euchromatin tend to be transcriptionally active?

a.) It contains mutations

b.) It lacks histones

c.) DNA is more accessible

d.) It is highly condensed

15
New cards

Acetylation opens chromatin; methylation often compacts it

How do histone acetylation and methylation differ in gene regulation?

a.) Both alter DNA sequence

b.) Both block transcription

c.) Both compact chromatin

d.) Acetylation opens chromatin; methylation often compacts it

16
New cards

They allow strong but reversible interactions

Why are non-covalent interactions ideal for protein–ligand binding?

a.) They allow strong but reversible interactions

b.) They form peptide bonds

c.) They require ATP hydrolysis

d.) They permanently lock ligands in place

17
New cards

They carry positive charges that bind DNA

Why are histones rich in lysine and arginine? 

a.) They form hydrogen bonds with RNA

b.) They degrade DNA

c.) They carry positive charges that bind DNA

d.) They repel DNA

18
New cards

Their hypervariable loops differ in amino acid sequence

Why can antibodies recognize billions of different antigens

a.) Their hypervariable loops differ in amino acid sequence

b.) They bind antigens covalently

c.) They contain multiple cofactors

d.) They are encoded by multiple genes

19
New cards

Reduced ligand-binding specificity

A mutation alters several amino acid side chains within a protein’s binding site. Which outcome is most likely?

a.) Complete loss of protein synthesis

b.) Reduced ligand-binding specificity

c.) Increased protein stability

d.) Increased transcription of the protein

20
New cards

Nucleosome

What is the basic unit of chromatin structure?

a.) Nucleosome

b.) Chromatid

c.) Centromere

d.) Histone tail