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Chapter 31: Problem 3

Protein molecules, like all molecules, can be characterized in terms of general properties such as size, shape, charge, solubility/hydrophobicity, Consider the influence of each of these general features on the likelihood of whether folding of a particular protein will require chaperone assistance or not. Be specific regarding just Hsp 70 chaperones or Hsp 70 chaperones and Hsp 60 chaperonins.

Short Answer

Expert verified
Whether a protein will require chaperone assistance for folding depends on its size, shape, charge, and solubility/hydrophobicity. Larger proteins, proteins with complex shapes, those with uneven charge distribution, and hydrophobic or less soluble proteins often require the assistance of Hsp70 or Hsp60 chaperones.

Step by step solution

01

Identifying the Influence of Size

The size of a protein can significantly impact folding. Smaller proteins can occasionally fold without assistance, while larger proteins typically require assistance from Hsp70 to ensure correct folding, preventing them from aggregating or misfolding.
02

Understanding the Impact of Shape

The shape of a protein can also influence folding. Certain geometries may create complex folding pathways or hidden hydrophobic cores requiring the assistance of Hsp70 or even further assistance from chaperonins like Hsp60 to correctly fold and maintain their active conformation.
03

Evaluating Charge Influence

Having unevenly distributed charges can create folding challenges as regions of like-charges repel each other. Hsp70 or Hsp60 can aid in managing these charges and ensuring the correct folding process.
04

Discussing the Role of Solubility/Hydrophobicity

Proteins with higher hydrophobicity or lesser solubility often require chaperones. Hsp70 can prevent hydrophobic aggregation, whereas Hsp60 can assist in the correct folding of these hydrophobic proteins.

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Most popular questions from this chapter

Not only is the Sec61p translocon complex essential for translocation of proteins into the ER lumen, it also mediates the incorporation of integral membrane proteins into the ER membrane. The mechanism for integration is triggered by stop-transfer signals that cause a pause in translocation. Figure 31.5 shows the translocon as a closed cylinder spanning the membrane. Suggest a mechanism for lateral transfer of an integral membrane protein from the protein-conducting channel of the translocon into the hydrophobic phase of the ER membrane.

The amino acid sequence deduced from the nucleotide sequence of a newly discovered human gene begins: MRSLLILVLCFLPLAALGK ... Is this a signal sequence? If so, where does the signal peptidase act on it? What can you surmise about the intended destination of this protein?

HtrA proteases are dual-function chaperone-protease protein quality control systems. The protease activity of HtrA proteases depends on a proper spatial relationship between the Asp-His-Ser catalytic triad. Propose a mechanism for the temperature-induced switch of HtrA proteases from chaperone function to protease function.

A common post-translational modification is removal of the universal N-terminal methionine in many proteins by Met-aminopeptidase. How might Met removal affect the half-life of the protein?

The GroEL ring has a 5 -nm central cavity. Calculate the maximum molecular weight for a spherical protein that can just fit in this cavity, assuming the density of the protein is \(1.25 \mathrm{g} / \mathrm{mL}\)
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