Exam 4: The Three-Dimensional Structure of Proteins

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In a classic experiment by Christian Anfinsen in the 1950s, it was shown that ribonuclease A could be denatured and then refolded into a catalytically active protein. What control experiment demonstrated that ribonuclease A did not need a chaperone to become properly folded?

(Short Answer)

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Question 21

Which statement concerning the process of spontaneous folding of proteins is FALSE?

(Multiple Choice)

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Question 22

Interactions between residues on separate polypeptide chains could be best classified as _____ structure.

(Multiple Choice)

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Question 23

Which statement is NOT an appropriate description for van der Waals interactions?

(Multiple Choice)

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Question 24

Describe three of the important features of a $\beta$ sheet polypeptide structure. Provide one or two sentences for each feature.

(Essay)

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Question 25

A D-amino acid would interrupt an $\alpha$ helix made of L-amino acids. Another naturally occurring hindrance to the formation of an $\alpha$ helix is the presence of:

(Multiple Choice)

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Question 26

Intrinsically disordered proteins may:

(Multiple Choice)

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Question 27

Where are the hydrogen bonding typically found between two residues in an $\alpha$ helix?

(Short Answer)

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Question 28

Which backbone arrangement BEST represents that of two peptide bonds?

(Multiple Choice)

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Question 29

Each of the following reagents or conditions will denature a protein. For each, describe in one or two sentences what the reagent/condition does to destroy native protein structure. (a) urea (b) high temperature (c) detergent (d) low pH

(Short Answer)

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Question 30

Which method would NOT increase the strength of a fibrous protein?

(Multiple Choice)

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Question 31

Describe the quaternary structure of hemoglobin.

(Essay)

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Question 32

The $\alpha$ -keratin chains indicated by the diagram below have undergone one chemical step. To alter the shape of the $\alpha$ -keratin chains-as in hair waving-what subsequent steps are required? $The \alpha -keratin chains indicated by the diagram below have undergone one chemical step. To alter the shape of the \alpha -keratin chains-as in hair waving-what subsequent steps are required?$

(Multiple Choice)

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Question 33

Identify and quantify the secondary structures present in this protein:

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Question 34

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Provide a brief explanation for the statement "Soluble globular proteins can be distinguished from soluble intrinsically disordered proteins on the basis of their amino acid content."

(Short Answer)

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Question 35

In superhelical proteins, such as collagen, several polypeptide helices are intertwined. What is the function of this superhelical twisting?

(Short Answer)

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Question 36

In the diagram below, the plane drawn behind the peptide bond indicates the:

(Multiple Choice)

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Question 37

Proline residues are infrequently found in _ due to their _.

(Multiple Choice)

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Question 38

Which pairs of bonds within a peptide backbone show free rotation around both bonds?

(Multiple Choice)

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Question 39

The _ secondary structure is formed more readily than other types of secondary structures, most likely due to _.

(Multiple Choice)

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Question 40

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Exam 4: The Three-Dimensional Structure of Proteins

In a classic experiment by Christian Anfinsen in the 1950s, it was shown that ribonuclease A could be denatured and then refolded into a catalytically active protein. What control experiment demonstrated that ribonuclease A did not need a chaperone to become properly folded?

Which statement concerning the process of spontaneous folding of proteins is FALSE?

Interactions between residues on separate polypeptide chains could be best classified as _____ structure.

Which statement is NOT an appropriate description for van der Waals interactions?

Describe three of the important features of a β\betaβ sheet polypeptide structure. Provide one or two sentences for each feature.

A D-amino acid would interrupt an α\alphaα helix made of L-amino acids. Another naturally occurring hindrance to the formation of an α\alphaα helix is the presence of:

Intrinsically disordered proteins may:

Where are the hydrogen bonding typically found between two residues in an α\alphaα helix?

Which backbone arrangement BEST represents that of two peptide bonds?

Each of the following reagents or conditions will denature a protein. For each, describe in one or two sentences what the reagent/condition does to destroy native protein structure. (a) urea (b) high temperature (c) detergent (d) low pH

Which method would NOT increase the strength of a fibrous protein?

Describe the quaternary structure of hemoglobin.

The α\alphaα -keratin chains indicated by the diagram below have undergone one chemical step. To alter the shape of the α\alphaα -keratin chains-as in hair waving-what subsequent steps are required?

Identify and quantify the secondary structures present in this protein:

Provide a brief explanation for the statement "Soluble globular proteins can be distinguished from soluble intrinsically disordered proteins on the basis of their amino acid content."

In superhelical proteins, such as collagen, several polypeptide helices are intertwined. What is the function of this superhelical twisting?

In the diagram below, the plane drawn behind the peptide bond indicates the:

Proline residues are infrequently found in _____ due to their _____.

Which pairs of bonds within a peptide backbone show free rotation around both bonds?

The _____ secondary structure is formed more readily than other types of secondary structures, most likely due to _____.

The Foundations of Biochemistry

Water

Amino Acids, Peptides, and Proteins

Protein Function

Enzymes

Carbohydrates and Glycobiology

Nucleotides and Nucleic Acids

DNA-Based Information Technologies

Lipids

Biological Membranes and Transport

Biosignaling

Bioenergetics and Biochemical Reaction Types

Glycolysis, Gluconeogenesis, and the Pentose Phosphate Pathway

Principles of Metabolic Regulation

The Citric Acid Cycle

Fatty Acid Catabolism

Amino Acid Oxidation and the Production of Urea

Oxidative Phosphorylation and Photophosphorylation

Carbohydrate Biosynthesis in Plants and Bacteria

Lipid Biosynthesis

Biosynthesis of Amino Acids, Nucleotides, and Related Molecules

Hormonal Regulation and Integration of Mammalian Metabolism

Genes and Chromosomes

DNA Metabolism

RNA Metabolism

Protein Metabolism

Regulation of Gene Expression

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Describe three of the important features of a $\beta$ sheet polypeptide structure. Provide one or two sentences for each feature.

A D-amino acid would interrupt an $\alpha$ helix made of L-amino acids. Another naturally occurring hindrance to the formation of an $\alpha$ helix is the presence of:

Where are the hydrogen bonding typically found between two residues in an $\alpha$ helix?

Proline residues are infrequently found in _ due to their _.

The _ secondary structure is formed more readily than other types of secondary structures, most likely due to _.