Protein Folding Objective Type Questions & Answers

Questions

21 Experiments on denaturation and renaturation after the reduction andreoxidation of the —S—S— bonds in the enzyme ribonuclease (RNase) have shown that:

A folding of denatured RNase into the native, active conformation, requires the input of energy in the form of heat.

B native ribonuclease does not have a unique secondary and tertiary structure.

C the completely unfolded enzyme, with all —S—S— bonds broken, is still enzymatically active.

D the primary sequence of RNase is sufficient to determine its specific secondary and tertiary structure.

View Answer

Answer: the primary sequence of RNase is sufficient to determine its specific secondary and tertiary structure.

22 Which of the following is not known to be involved in the process of assisted folding of proteins?

A Peptide bond hydrolysis

B Heat shock proteins

C Disulfide interchange

D Chaperonins

View Answer

Answer: Peptide bond hydrolysis

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23 Protein S will fold into its native conformation only when protein Q is also present in the solution. However, protein Q can fold into its native conformation without protein S. Protein Q, therefore, may function as a ---------- for protein S.

A ligand

B molecular chaperone

C protein precursor

D structural motif

View Answer

Answer: molecular chaperone

24 Which of the following statements concerning the process of spontaneous folding of proteins is false?

A It may be an essentially random process.

B It may be defective in some human diseases.

C It may involve a gradually decreasing range of conformational species.

D It may involve initial formation of a highly compact state.

View Answer

Answer: It may be an essentially random process.

25 Chaperone proteins function by

A providing a protective environment in which proteins can fold properly

B degrading proteins that have folded improperly

C providing a template for how the proteins should fold

D rescuing proteins that folded incorrectly and allowing them to refold into proper configuration

View Answer

Answer: rescuing proteins that folded incorrectly and allowing them to refold into proper configuration

26 Which of the following is least likely to result in protein denaturation?

A Altering net charge by changing pH

B Changing the salt concentration

C Disruption of weak interactions by boiling

D Exposure to detergents

View Answer

Answer: Changing the salt concentration

27 An average protein will not be denatured by:

A a detergent such as sodium dodecyl sulfate (SDS).

B heating to 90°C.

C iodoacetic acid.

D pH 10.

View Answer

Answer: heating to 90°C.

28 PDI is an enzyme involve in

A Protein synthesis

B Protein degradation

C Protein folding

D Protein quaternery structure formation

View Answer

Answer: Protein folding

29 Which of the following amino acids are rarely present in alpha helix

A Glycine and proline

B Proline and tryptophan

C Tryptophan and glycine

D Proline only

View Answer

Answer: Glycine and proline

30 Αlpha-helix has

A 3.6 residues/turn and is a right handed helix

B 3.8 residues/turn and is a right handed helix

C 3.6 residues/turn and is a left handed helix

D 3.8 residues/turn and is a left handed helix

View Answer

Answer: 3.6 residues/turn and is a right handed helix

31 All the statements regarding peptide bond are true except

A Peptide bond is a co-valent bond

B Peptide bond is rigid and planar

C Peptide bond has partial double bond character

D Peptide bond is formed by non-condensation reaction

View Answer

Answer: Peptide bond is formed by non-condensation reaction

32 EF-1α and EF-Tu are

A Analogs

B Homologs

C Paralogs

D Syllogs

View Answer

Answer: Homologs

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