The sharp transition seen in Figure suggests that

A. Proteins can be denatured by any treatment that disrupts the weak bonds stabilizing tertiary structure, such as heating, or by chemical denaturants such as urea or guanidinium chloride.

B. A comparison of the degree of unfolding as the concentration of denaturant increases reveals a sharp transition from the folded, or native, form to the unfolded, or denatured form, suggesting that only these two conformational states are present to any significant extent.

C. A similar sharp transition is observed if denaturants are removed from unfolded proteins, allowing the proteins to fold.

D. Protein folding and unfolding is an “all or none” process that results from a cooperative transition .

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#Question id: 4241

#Unit 3. Fundamental Processes

Use the figure to answer the question. The tRNA shown in the figure has its 3′ end projecting beyond its 5′ end. Which of the following processes will occur at this 3′ end?

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#Question id: 1536

#Unit 4. Cell Communication and Cell Signaling

Use the following figure to answer the question. According to figure, which of the following statement is incorrect?

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#Question id: 33289

#Unit 2. Cellular Organization

The instability of p53 results from its ubiquitinylation by a ubiquitin-protein ligase called:

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#Question id: 3690

#Unit 3. Fundamental Processes

The DNA polymerase is a template-directed enzyme that synthesizes new complementary strand from a parent strand but it requires the existing short nucleotide sequence for its elongation. Which of the following enzyme is required for the synthesis of this primer?

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#Question id: 4308

#Unit 3. Fundamental Processes

Most repressor proteins are allosteric. Which of the following molecules binds with the repressor to alter its conformation and therefore affect its function?