/*! This file is auto-generated */ .wp-block-button__link{color:#fff;background-color:#32373c;border-radius:9999px;box-shadow:none;text-decoration:none;padding:calc(.667em + 2px) calc(1.333em + 2px);font-size:1.125em}.wp-block-file__button{background:#32373c;color:#fff;text-decoration:none} Problem 69 Multidomain proteins tend to fol... [FREE SOLUTION] | 91影视

91影视

Log out

Learning Materials

Features

Discover

Chapter 22: Problem 69

Multidomain proteins tend to fold better inside cagelike chaperonin structures (such as GroEL/GroES in E. coli) than with cytosolic chaperones. Explain why.

Short Answer

Expert verified
Chaperonins provide an isolated environment, preventing aggregation and misfolding, crucial for folding complex multidomain proteins.

Step by step solution

01

Understand the Structure of Chaperonins

Chaperonins are specialized proteins, often forming large cylindrical structures, that provide an isolated environment for protein folding. In Escherichia coli, the GroEL/GroES complex is a well-known chaperonin system.
02

Consider the Environment Provided by Chaperonins

Chaperonins offer a secluded space where polypeptide chains can fold without interference from other cellular components. This environment is favorable for the proper folding of complex proteins by preventing aggregation and misfolding that can occur due to interactions with other molecules in the cytosol.
03

Examine the Nature of Multidomain Proteins

Multidomain proteins consist of several distinct regions or domains that must fold and align correctly to function properly. These proteins have a higher degree of complexity and surface area, increasing the chance of improper interactions or aggregation in a crowded cytosolic environment.
04

Analyze the Benefits of Chaperonin Structures for Multidomain Proteins

The cagelike structure of chaperonins helps isolate multidomain proteins from the cytosolic milieu, reducing incorrect interactions and promoting correct domain folding. The encapsulated space allows sequential folding of domains and prevents aggregation, which aids in achieving the correct native state.

Unlock Step-by-Step Solutions & Ace Your Exams!

  • Full Textbook Solutions

    Get detailed explanations and key concepts

  • Unlimited Al creation

    Al flashcards, explanations, exams and more...

  • Ads-free access

    To over 500 millions flashcards

  • Money-back guarantee

    We refund you if you fail your exam.

Over 30 million students worldwide already upgrade their learning with 91影视!

Key Concepts

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

Protein Folding
Protein folding is a fundamental biological process where a protein chain acquires its functional shape or conformation. It is an essential step for proteins to become biologically active and perform their functions accurately.
Misfolding can lead to dysfunction or aggregation, potentially causing diseases such as Alzheimer's and Parkinson's.

Several factors influence the folding process:
  • Primary amino acid sequence - dictates the protein's final shape.
  • Cellular environment - components like water, ions, and pH levels play a critical role.
  • Folding influences - support from molecular "chaperones," which assist proteins in reaching their correct structure.
Proteins often fold spontaneously, but complex proteins, especially those with multiple domains, may need help from chaperonins to avoid competing interactions and reach their proper form correctly.
Multidomain Proteins
Multidomain proteins, as the name suggests, are composed of multiple structural units called domains. Each domain typically performs a distinct chemical function.
These proteins are greater in complexity compared to single-domain proteins due to the need for proper domain alignment and interaction.

Key characteristics of multidomain proteins include:
  • Multiple folding regions - each domain folds into its characteristic three-dimensional shape.
  • Inter-domain interactions - coordination is crucial to ensure that the domains layer correctly.
  • Increased susceptibility to error - high surface area and complex folding require stringent regulation.
Because of these challenges, chaperonins, such as the GroEL/GroES complex, often aid in correctly folding these proteins, providing a private and organized space for proper folding.
GroEL/GroES Complex
The GroEL/GroES complex is a prominent example of chaperonin systems found in the bacterium *E. coli*. It consists of two main components, GroEL and GroES, working as a team to assist in protein folding.
GroEL forms a double-ring cylinder structure, creating a cage-like environment that encapsulates unfolded polypeptides.

Here's how this complex facilitates protein folding:
  • Isolation - the cage prevents inappropriate interactions with other molecules.
  • Assisted folding - confines the protein, reducing the risk of misfolding and aggregation.
  • Sequential operation - allows folding to occur in an ordered manner, cycling through different conformations.
The GroES "cap" assists by sealing the cylinder, ensuring a controlled environment where the polypeptide can refold until it reaches its stable, functional form, making it particularly effective for complex proteins.

One App. One Place for Learning.

All the tools & learning materials you need for study success - in one app.

Get started for free

Most popular questions from this chapter

The protein c-Myc is a leucine zipper protein that regulates gene expression in cell proliferation and differentiation. Its activity was known to be regulated by phosphorylation of a specific threonine residue, but later studies showed that this same threonine could be modified by an \(N\)-acetylglucosamine residue and that phosphorylation and glycosylation were competitive processes. The specific threonine is mutated in some human lymphomas. Draw the structure of the \(O\)-glycosylated threonine residue.

Ribosomal inactivating proteins (RIPs) are RNA \(N\)-glycosidases found in plants. They catalyze the hydrolysis of specific adenine residues in RNA. RIPs are highly toxic but might be useful as antitumor drugs because ribosome synthesis is upregulated in transformed cells. Give a general explanation that describes how RIPs inactivate ribosomes.

The sequences for all the ribosomal proteins in \(E\). coli have been elucidated and have been found to contain large amounts of lysine and arginine residues. Why is this finding not surprising? What kinds of interactions are likely to form between the ribosomal proteins and the ribosomal RNA?

Identify which terms are associated with transcription and which with translation: a. Promoter; b. TATA box; c. Shine-Dalgarno sequence; d. \(\sigma\) factor; e. \(-35\) region; f. \(\mathrm{AUG}\) codon; \(\mathrm{g}\). downstream promoter element (DPE).

A new tRNA discovered in \(E\). coli contains a uridine modified to form uridine- \(5^{\prime}\)-oxyacetic acid (cmo \({ }^{5} \mathrm{U}\) ). The modified uridine can base pair with \(\mathrm{G}, \mathrm{A}\), and U. What mRNA codons are recognized by tRNA \({ }_{c m o}^{L} \mathrm{UAG}^{2}\) ?
See all solutions

Recommended explanations on Chemistry Textbooks

Physical Chemistry

Read Explanation

Organic Chemistry

Read Explanation

Chemical Analysis

Read Explanation

Kinetics

Read Explanation

Inorganic Chemistry

Read Explanation

Nuclear Chemistry

Read Explanation
View all explanations

What do you think about this solution?

We value your feedback to improve our textbook solutions.

Study anywhere. Anytime. Across all devices.