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Chaperones A. are always required to direct the folding of proteins. B. when bound to protcin increase the rate of protein degradation. C. usually bind to strongly hydrophilic regions of unfolded proteins. D. sometimes maintain proteins in an unfolded state to allow passage through membranes. E. foster aggregation of proteins into plaques.

Short Answer

Expert verified
Answer: The primary function of chaperones is to assist in the correct folding of other proteins and prevent misfolding and aggregation. The true statement is: "Chaperones sometimes maintain proteins in an unfolded state to allow passage through membranes."

Step by step solution

01

Definition of Chaperones and their Function

Chaperones are proteins that assist in the correct folding of other proteins. They prevent misfolding and aggregation (clumping together) of proteins, which can lead to diseases or cellular malfunction. Now let's go through each statement and determine if it is true or false.
02

Statement A

This statement claims that chaperones are always required to direct the folding of proteins. While chaperones play an important role in assisting with protein folding, not all proteins require chaperones for this process. Some proteins can fold spontaneously without assistance. Statement A is false.
03

Statement B

This statement claims that chaperones, when bound to proteins, increase the rate of protein degradation. Chaperones indeed bind to proteins, but their primary function is assisting in protein folding, not degradation. Statement B is false.
04

Statement C

This statement claims that chaperones usually bind to strongly hydrophilic regions of unfolded proteins. Chaperones typically bind to hydrophobic regions to prevent aggregation and assist in proper folding. Statement C is false.
05

Statement D

This statement claims that chaperones sometimes maintain proteins in an unfolded state to allow passage through membranes. In some cases, chaperones can prevent a protein from folding or help unfold it, allowing it to pass through a membrane. This is true for certain cellular compartments, such as the mitochondria, where proteins must cross the membrane in an unfolded state. Statement D is true.
06

Statement E

This statement claims that chaperones foster aggregation of proteins into plaques. This is the exact opposite of chaperones' primary function, which is to prevent misfolding and aggregation. Statement E is false. Based on our analysis, the correct choice is: D. Chaperones sometimes maintain proteins in an unfolded state to allow passage through membranes.

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Key Concepts

These are the key concepts you need to understand to accurately answer the question.

Protein Folding
Understanding the process of protein folding is fundamental to appreciating how life at a cellular level functions. Proteins are complex molecules that perform a wide variety of functions within living organisms, and their functionality is deeply tied to their three-dimensional shape. This intricate process is driven by the primary amino acid sequence encoded by genes, whereby a polypeptide chain naturally assumes a specific, stable structure, known as its native conformation.

However, protein folding is not always straightforward. Sometimes, proteins can misfold, leading to dysfunctional forms that may aggregate, potentially causing diseases such as Alzheimer's or Parkinson's. Chaperones, therefore, are essential in guiding proteins to fold correctly and maintaining cellular health. By ensuring proteins achieve their proper structure, chaperones play a significant role in the overall dynamics of cellular mechanisms, ultimately impacting an organism's wellbeing.
Cellular Mechanisms
Cellular mechanisms encompass the numerous processes that occur within cells to sustain life, including replication, energy conversion, and the synthesis of biomolecules. Within this realm, protein chaperones work as part of the cellular quality control system, monitoring and aiding the correct folding of proteins. Their presence is a testament to the evolutionary refinement of cellular processes, where efficiency and error mitigation are paramount.

For example, when a protein must traverse a membrane to reach the location where it will function, chaperones may hold it in an unfolded state to facilitate its passage. This careful orchestration demonstrates the versatility and specificity of chaperones within cellular mechanisms. Understanding these processes, from synthesis to post-translational modification, provides a clear picture of the meticulous orchestration inherent in cellular biology—and protein chaperones are integral to that picture.
Biochemistry Education
Biochemistry education involves imparting knowledge on the chemical processes and substances that occur in living organisms. It is a field that demands clear understanding of complex concepts, such as the role of protein chaperones in maintaining protein homeostasis. Educators in biochemistry strive to break down these intricate topics into comprehensible segments for students to easily grasp.

For instance, in examining the role of protein chaperones, it's important to emphasize the conditions under which these molecules operate and their significance in the broader context of cellular function. By encouraging students to explore why some proteins need chaperones while others do not, or how chaperones can prevent disease-related protein aggregations, we cultivate critical thinking and a deeper appreciation for the elegance of biochemical processes. Utilizing resources such as illustrative animations, interactive models, and real-life examples, biochemistry education can effectively bring to light the multifaceted roles that proteins and their helpers, the chaperones, play in life's molecular dance.

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Most popular questions from this chapter

Chaperones A. are always required to direct the folding of proteins. B. when bound to protein increase the rate of protein degradation. C. usually bind to strongly hydrophilic regions of unfolded proteins. D. sometimes maintain proteins in an unfolded state to allow passage through membranes. E. foster aggregation of proteins into plaques.

I-Cell paticnts lack the enzyme that transfers N-acetylglucosamine phosphate to high mannose type oligosaccharides on the protein. This \(N\) -linked glycosylation A. occurs only after the protein has been completely translated and folded. B. does not require any specific amino acid sequence. C. occurs by transfer of an oligosaccharide chain from a dolichol phosphate carrier to the protcin. D. has the oligosaccharide chain attached to serine or threonine. E. contains only mannoses in the chain.

Formation of mature insulin includes all of the following except A. removal of a signal peptide. B. folding into a three-dimensional structure. C. disulfide bond formation. D. removal of a peptide from an internal region. E. \(\gamma\) -carboxylation of glutamate residues.

In the formation of an aminoacyl-tRNA, A. ADP and Pi are products of the reaction. B. aminoacyl adenylate appears in solution as a free intermediate. C. aminoacyl-tRNA synthetase is believed to recognize and hydrolyze incorrect aminoacyl-tRNAs it may have produced. D. separate aminoacyl-tRNA synthetases exist for cvery amino acid in the functional protein. E. there is a scparate aminoacyl-tRNA synthetase for crery tRNA species.

Much of procollagen formation occurs in the endoplasmic reticulum and Golgi apparatus which requires signal peptide. All of the following statements about targeting a protein for the ER are true except A. signal peptide usually has a positively charged N-terminus and a stretch of hydrophobic amino acids. B. signal peptide emerging from a free ribosome binds signal recognition particle (SRP). C. signal peptide is usually cleaved from the protein before the protein is inserted into the ER membrane. D. docking protein is actually an SRP receptor and serves to bind the SRP to the ER. E. \(\operatorname{SRP}\) and docking protein do not enter the ER lumen but are recycled.

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