Biochem Chapter 4 part 2

What are some functions of globular proteins, and how do they contribute to cellular processes?

• They primarily provide structural support to cells.

• They act as enzymes, transport molecules, and play roles in cell signaling.

• They are involved in the storage of genetic information.

• They form the lipid bilayer of cell membranes.

Explain the difference between a motif and a domain in protein structure. Why is this distinction important in understanding protein function?

• A motif is a large, independently stable structure, while a domain is a small, recurring sequence.

• A motif is a small, recurring sequence, while a domain is a large, independently stable structure.

• Both motifs and domains are large, independently stable structures.

• Both motifs and domains are small, recurring sequences.

How does entropy change during protein folding, and what implications does this have for the stability of the folded protein?

• Entropy increases, leading to a more stable folded state.

• Entropy decreases, leading to a more stable folded state.

• Entropy remains constant, having no effect on stability.

• Entropy decreases, leading to an unstable folded state.

Discuss the characteristics of protein folding and how they ensure proper protein function.

• Protein folding is random and does not affect function.

• Protein folding is a highly ordered process that ensures functional conformation.

• Protein folding is a reversible process that leads to denaturation.

• Protein folding is independent of the amino acid sequence.

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NGSS.HS-LS1-1

What are the consequences of protein misfolding, and how can this affect cellular health?

• Misfolded proteins are always beneficial and enhance cellular function.

• Misfolded proteins can lead to diseases such as Alzheimer's and Parkinson's.

• Misfolded proteins are easily corrected by the cell without any consequences.

• Misfolded proteins have no impact on cellular health.

Define proteostasis and explain its significance in maintaining cellular function.

• Proteostasis refers to the degradation of proteins in the cell.

• Proteostasis is the process of protein synthesis only.

• Proteostasis involves the regulation of protein folding, maintenance, and degradation.

• Proteostasis is unrelated to protein function.

Describe the methods by which proteins can be denatured and the impact of denaturation on protein function.

• Proteins can be denatured by heat, pH changes, and chemicals, leading to loss of function.

• Proteins can only be denatured by heat, with no impact on function.

• Proteins can be denatured by light exposure, enhancing their function.

• Proteins cannot be denatured by any means.

What happens to the four levels of protein structure when they are unfolded through denaturation?

• Only the primary structure is affected, while others remain intact.

• All levels, including primary, secondary, tertiary, and quaternary, are disrupted.

• Only the quaternary structure is affected, while others remain intact.

• Denaturation does not affect any level of protein structure.

What are intrinsically unstructured proteins, and why are they important in cellular processes?

• They are proteins with a fixed structure, important for rigidity.

• They lack a fixed structure, allowing flexibility in interactions and functions.

• They are proteins that do not exist in cells.

• They are proteins that only function outside the cell.

Analyze the role of intrinsically unstructured proteins in disease mechanisms and therapeutic strategies.

• They have no role in disease mechanisms or therapeutic strategies.

• Their flexibility can lead to aggregation, contributing to diseases, but also offers targets for therapy.

• They are always beneficial and prevent diseases.

• They are only involved in non-disease-related processes.