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Part A Why does it make biochemical sense that chaperones recognize hydrophobic surface area? What catastrophic event are chaperones meant to prevent in cells? Match the items in the left column to the appropriate blanks in the sentences on the right. recognition reversible protein denaturation hydrophilic A folded excessive protein folding hydrophobic irreversible aggregation of unfolded proteins transport of proteins from the cytoplasm An unfolded folding Chaperones are meant to prevent of surfaces. area. Thus, as proteins unfold, more by chaperones. Reset Help which is mediated by the intermolecular association protein will minimize solvent-exposed surface area will be exposed, triggering surface

Part A Why does it make biochemical sense that chaperones recognize hydrophobic surface area? What catastrophic event are chaperones meant to prevent in cells? Match the items in the left column to the appropriate blanks in the sentences on the right. recognition reversible protein denaturation hydrophilic A folded excessive protein folding hydrophobic irreversible aggregation of unfolded proteins transport of proteins from the cytoplasm An unfolded folding Chaperones are meant to prevent of surfaces. area. Thus, as proteins unfold, more by chaperones. Reset Help which is mediated by the intermolecular association protein will minimize solvent-exposed surface area will be exposed, triggering surface

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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**Educational Content: Understanding Chaperones and Protein Folding** **Topic:** Chaperones in Biochemistry Chaperones play a crucial role in cellular processes by recognizing and addressing improper protein folding. They are responsible for preventing catastrophic events such as the irreversible aggregation of unfolded proteins. This process is mediated by the intermolecular association of hydrophobic surfaces. Proteins are composed of both hydrophobic and hydrophilic regions. In a properly folded protein, hydrophobic regions are typically hidden from solvent exposure to maintain structural stability. However, during protein unfolding, these hydrophobic regions become exposed. This exposure increases the risk of proteins aggregating irreversibly. Chaperones function by binding to these exposed hydrophobic surfaces, minimizing their solvent exposure and preventing aggregation. This intervention ensures proteins can refold correctly or be directed for degradation if necessary. **Sentence Structure:** - Chaperones are meant to prevent **irreversible aggregation of unfolded proteins**, which is mediated by the intermolecular association of **hydrophobic** surfaces. - **A folded** protein will minimize solvent-exposed **hydrophobic** surface area. - Thus, as proteins unfold, more **hydrophobic** surface area will be exposed, triggering **recognition** by chaperones. Understanding how chaperones work is critical for comprehending how cells maintain protein homeostasis and prevent diseases associated with protein misfolding, such as Alzheimer's.
Transcribed Image Text:**Educational Content: Understanding Chaperones and Protein Folding** **Topic:** Chaperones in Biochemistry Chaperones play a crucial role in cellular processes by recognizing and addressing improper protein folding. They are responsible for preventing catastrophic events such as the irreversible aggregation of unfolded proteins. This process is mediated by the intermolecular association of hydrophobic surfaces. Proteins are composed of both hydrophobic and hydrophilic regions. In a properly folded protein, hydrophobic regions are typically hidden from solvent exposure to maintain structural stability. However, during protein unfolding, these hydrophobic regions become exposed. This exposure increases the risk of proteins aggregating irreversibly. Chaperones function by binding to these exposed hydrophobic surfaces, minimizing their solvent exposure and preventing aggregation. This intervention ensures proteins can refold correctly or be directed for degradation if necessary. **Sentence Structure:** - Chaperones are meant to prevent **irreversible aggregation of unfolded proteins**, which is mediated by the intermolecular association of **hydrophobic** surfaces. - **A folded** protein will minimize solvent-exposed **hydrophobic** surface area. - Thus, as proteins unfold, more **hydrophobic** surface area will be exposed, triggering **recognition** by chaperones. Understanding how chaperones work is critical for comprehending how cells maintain protein homeostasis and prevent diseases associated with protein misfolding, such as Alzheimer's.
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