Biochem Proteins

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Pharmdnate

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Quizzes Created: 22 | Total Attempts: 109,869

Questions: 10 | Attempts: 4,164 | Updated: Mar 21, 2023

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Quiz on biochem. 10 questions about proteins.

Questions and Answers

1.

What are short polypeptides called?
- A.
  
  Primary structures
- B.
  
  Secondary structures
- C.
  
  Polypeptides
- D.
  
  Oligopeptides
Correct Answer
D. Oligopeptides

Explanation
Oligopeptides are short polypeptides consisting of a small number of amino acids. They are smaller than polypeptides but larger than peptides. Oligopeptides play important roles in various biological processes, such as hormone regulation and cell signaling. They are formed through the process of peptide bond formation between amino acids. Therefore, oligopeptides are the correct term for short polypeptides.

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2.

What is comprised of alpha-helices or parallel or antiparallel beta-pleated sheets?
- A.
  
  Primary structures
- B.
  
  Secondary structures
- C.
  
  Both A and B
- D.
  
  None of the above
Correct Answer
B. Secondary structures

Explanation
Secondary structures in proteins are comprised of alpha-helices or parallel or antiparallel beta-pleated sheets. The primary structure of a protein refers to the sequence of amino acids in the polypeptide chain, while the secondary structure refers to the local folding patterns that arise due to hydrogen bonding between nearby amino acids. These folding patterns can include alpha-helices, which are coiled structures, or beta-pleated sheets, which are formed by extended strands of amino acids. Therefore, the correct answer is secondary structures.

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3.

At what amino acids can beta-turns occur?
- A.
  
  Glycine and alanine
- B.
  
  Glycine and proline
- C.
  
  Glutamate and proline
- D.
  
  Glutamate and alanine
Correct Answer
B. Glycine and proline

Explanation
Beta-turns are secondary structural motifs in proteins where the polypeptide chain reverses direction. They are commonly found at two specific amino acids: glycine and proline. Glycine is the smallest amino acid and lacks a side chain, allowing for flexibility in the polypeptide chain. Proline, on the other hand, has a rigid structure due to the cyclic nature of its side chain, which promotes the formation of turns. Therefore, beta-turns can occur at glycine and proline residues in proteins.

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4.

Where can disulfide covalent linkages occur between adjacent alpha-helices?
- A.
  
  In keratin
- B.
  
  In the major protein of hair
- C.
  
  In nails
- D.
  
  All of the above
Correct Answer
D. All of the above

Explanation
Disulfide covalent linkages can occur between adjacent alpha-helices in keratin, the major protein of hair, and in nails. These linkages are formed between the sulfur atoms of two cysteine residues, creating a strong bond that contributes to the structural stability of these proteins. Therefore, the correct answer is "all of the above."

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5.

Which of the following is a incomplete dietary protein found in connective tissues?
- A.
  
  Collagen
- B.
  
  Keratin
- C.
  
  RNase A
- D.
  
  All of the above
Correct Answer
A. Collagen

Explanation
Collagen is an incomplete dietary protein found in connective tissues. It is considered incomplete because it lacks one or more essential amino acids required by the body. Collagen is a structural protein that provides strength and support to connective tissues such as tendons, ligaments, and skin. It is also found in bones, cartilage, and blood vessels. Keratin is another protein found in hair, nails, and skin, while RNase A is an enzyme. Therefore, the correct answer is collagen, as it is the only option that fits the given description.

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3
6.

What is the cause of scurvy?
- A.
  
  Not being exposed to enough sunlight
- B.
  
  Misfolding protiens
- C.
  
  Defective collagen formation
- D.
  
  All of the above
Correct Answer
C. Defective collagen formation

Explanation
Scurvy is caused by a deficiency of vitamin C, which is essential for the production of collagen. Collagen is a protein that helps in the formation of connective tissues, such as skin, blood vessels, and bones. Without enough vitamin C, the body is unable to produce healthy collagen, leading to the symptoms of scurvy. The other options mentioned, not being exposed to enough sunlight and misfolding proteins, are not directly related to the cause of scurvy.

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7.

What assists large proteins in folding?
- A.
  
  Prion (prp)
- B.
  
  Amyliod fibers
- C.
  
  Molecular chaperones
- D.
  
  All of the above
Correct Answer
C. Molecular chaperones

Explanation
Molecular chaperones assist large proteins in folding. They are a class of proteins that help other proteins achieve their correct three-dimensional structure. By interacting with unfolded or misfolded proteins, molecular chaperones prevent aggregation and promote proper folding, ensuring that proteins function correctly. This assistance is crucial for the proper functioning of many cellular processes. Both prions (prp) and amyloid fibers are not involved in assisting protein folding, making the correct answer "molecular chaperones."

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8.

What does type 2 diabetes, Alzheimer's disease, Huntinghton's disease and Parkinson's disease have in common?
- A.
  
  They are all forms of spongifoam encephalopathies
- B.
  
  They are caused by amyliodoses
- C.
  
  They are caused by low amounts of dopamine
- D.
  
  They are caused by excessive amounts of dopamine
Correct Answer
B. They are caused by amyliodoses

Explanation
Type 2 diabetes, Alzheimer's disease, Huntington's disease, and Parkinson's disease are all caused by amyliodoses. Amyliodoses refers to the accumulation of abnormal proteins, specifically amyloid proteins, in various tissues and organs of the body. In these diseases, amyloid proteins build up and form plaques or tangles, leading to dysfunction and damage in the affected tissues. This common factor of amyliodoses helps to explain the similarities in the pathogenesis and clinical features observed in these different diseases.

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9.

What disease results from the misfolding of prion (prp)?
- A.
  
  Crutzfeld Jacob Disease (CJD)
- B.
  
  Cystic Fibrosis
- C.
  
  Alzheimer's Disease
- D.
  
  All of the above
Correct Answer
A. Crutzfeld Jacob Disease (CJD)

Explanation
Crutzfeld Jacob Disease (CJD) is the correct answer because it is a disease that results from the misfolding of prion (prp). CJD is a rare and fatal degenerative brain disorder that affects memory, thinking, and movement. The misfolded prions accumulate in the brain, causing damage and leading to the characteristic symptoms of the disease. Cystic Fibrosis and Alzheimer's Disease are unrelated to the misfolding of prions and have different causes and symptoms. Therefore, the correct answer is CJD.

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10.

Which of the following are forms of spongifoam encephalopathies?
- A.
  
  Mad Cow Disease
- B.
  
  Kuru
- C.
  
  Scrapie
- D.
  
  All of the above
Correct Answer
D. All of the above

Explanation
All of the mentioned options, Mad Cow Disease, Kuru, and Scrapie, are forms of spongiform encephalopathies. Spongiform encephalopathies are a group of rare neurodegenerative diseases characterized by the accumulation of abnormal prion proteins in the brain, leading to the formation of sponge-like holes in the tissue. Mad Cow Disease affects cows, Kuru is found in humans, and Scrapie affects sheep and goats. Therefore, all of these options are correct forms of spongiform encephalopathies.

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Current Version
Mar 21, 2023

Quiz Edited by
ProProfs Editorial Team
Dec 27, 2010

Quiz Created by
Pharmdnate

Biochem Proteins

What are short polypeptides called?

What is comprised of alpha-helices or parallel or antiparallel beta-pleated sheets?

At what amino acids can beta-turns occur?

Where can disulfide covalent linkages occur between adjacent alpha-helices?

Which of the following is a incomplete dietary protein found in connective tissues?

What is the cause of scurvy?

What assists large proteins in folding?

What does type 2 diabetes, Alzheimer's disease, Huntinghton's disease and Parkinson's disease have in common?

What disease results from the misfolding of prion (prp)?

Which of the following are forms of spongifoam encephalopathies?