Protein Folding MCQs with Answers

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Protein Folding Online Quiz

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• Test Name: Protein Folding MCQ Quiz Practice
• Type: Quiz Test
• Total Questions: 40
• Total Marks: 40
• Time: 40 minutes

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Protein Folding

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1 / 40

What is the role of chaperone proteins?

Transport proteins

Degrade misfolded proteins

Assist in protein folding

2 / 40

What is a prion?

Infectious protein

Nucleic acid

Carbohydrate

3 / 40

What is the main driving force for protein folding?

Hydrophobic interactions

Hydrogen bonding

Covalent bonding

4 / 40

What disease is associated with protein misfolding and aggregation?

Diabetes

Alzheimer's disease

Hypertension

5 / 40

Which interaction is NOT involved in maintaining protein tertiary structure?

Hydrogen bonds

Phosphodiester bonds

Ionic bonds

6 / 40

What does CD spectroscopy measure in proteins?

Secondary structure

Protein concentration

Primary structure

7 / 40

What is the native state of a protein?

The functional 3D form

The unfolded form

The denatured form

8 / 40

Which factor can induce protein denaturation?

High pH

Heat

Low light

9 / 40

What term describes the overall 3D structure of a single protein molecule?

Tertiary structure

Secondary structure

Quaternary structure

10 / 40

What structure is characterized by alpha helices and beta sheets?

Quaternary structure

Secondary structure

Primary structure

11 / 40

What is protein crystallography used for?

Analyze protein function

Measure protein size

Determine 3D structure

12 / 40

Which type of protein structure involves the assembly of multiple polypeptide chains?

Tertiary structure

Secondary structure

Quaternary structure

13 / 40

What is an example of a post-translational modification affecting protein folding?

Phosphorylation

Translation

Transcription

14 / 40

What is the term for proteins that assist other proteins to fold correctly?

Chaperones

Receptors

Enzymes

15 / 40

What is the first step of protein folding?

Formation of quaternary structure

Formation of secondary structure

Protein denaturation

16 / 40

What technique can be used to monitor protein folding in real-time?

Fluorescence spectroscopy

PCR

Western blotting

17 / 40

What is the Levinthal's paradox in protein folding?

Protein folding is not random

All proteins fold at the same rate

Protein folding is spontaneous

18 / 40

What is the role of the proteasome?

Degrade misfolded proteins

Synthesize proteins

Transport proteins

19 / 40

Which structure is described by the sequence of amino acids in a protein?

Primary structure

Tertiary structure

Secondary structure

20 / 40

What determines the primary structure of a protein?

Type of chaperones

Sequence of amino acids

Presence of cofactors

21 / 40

What is the Anfinsen's dogma?

Proteins need chaperones

Proteins can refold independently

Protein sequence determines folding

22 / 40

Which amino acid is known as a helix breaker?

Proline

Glycine

Alanine

23 / 40

What happens during protein misfolding?

Increased stability

New functions are gained

Function is lost

24 / 40

What can mutations in the coding sequence of a protein lead to?

Increased expression

Correct folding

Misfolding

25 / 40

What term describes a protein's loss of its native structure?

Denaturation

Renaturation

Aggregation

26 / 40

What is the unfolded protein response?

Cellular stress response

Protein synthesis regulation

Formation of beta sheets

27 / 40

What is the significance of disulfide bonds in proteins?

Catalyze reactions

Stabilize protein structure

Signal transduction

28 / 40

What does the term "denaturation" refer to?

Synthesis of new proteins

Loss of 3D structure

Formation of peptide bonds

29 / 40

What can cause protein aggregation?

Gene expression

Correct folding

Misfolding

30 / 40

Which protein misfolding disease is characterized by the accumulation of amyloid plaques?

Cystic fibrosis

Parkinson's disease

Alzheimer's disease

31 / 40

What is the molten globule state in protein folding?

Intermediate state

Fully folded state

Unfolded state

32 / 40

What effect does pH have on protein folding?

Stabilizes disulfide bonds

Increases hydrophobic interactions

Alters ionic interactions

33 / 40

What technique is commonly used to determine protein structure?

Gel electrophoresis

Polymerase chain reaction

X-ray crystallography

34 / 40

What structural feature is common in transmembrane proteins?

Beta sheets

Random coils

Alpha helices

35 / 40

What is the significance of beta-turns in protein structure?

Forms the protein core

Stabilizes the tertiary structure

Connects alpha helices and beta sheets

36 / 40

Which molecule assists in protein folding by preventing aggregation?

Ribosome

ATP

Chaperone

37 / 40

What is the primary driving force behind the formation of alpha helices and beta sheets?

Ionic bonding

Covalent bonding

Hydrogen bonding

38 / 40

What does the term "protein folding funnel" refer to?

Protein synthesis process

Energy landscape of folding

Protein degradation pathway

39 / 40

Which type of bond is NOT commonly involved in stabilizing protein tertiary structure?

Disulfide bond

Phosphodiester bond

Hydrogen bond

40 / 40

What can be used to refold denatured proteins?

ATP

Chaperones

RNA

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