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In hydroxyl radical footprinting, regions with solvent accessibility are likely to be cleaved.

Short Answer

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Regions with high solvent accessibility are more likely to be cleaved in hydroxyl radical footprinting.

Step by step solution

01

Understanding the Concept

In hydroxyl radical footprinting, hydroxyl radicals are used to cleave DNA or protein segments. These segments are more likely to be cleaved in regions that are exposed to the solvent. This is because solvent-accessible areas are more exposed and thus more susceptible to attack by radicals.
02

Identifying Solvent Accessibility

Solvent accessibility refers to how much of a molecule's surface is exposed to the surrounding solvent, which is typically water in biochemical contexts. Molecules like proteins and DNA can have regions that are either highly solvent-accessible or buried and protected from solvent exposure.
03

Relating Solvent Accessibility to Cleavage

The mechanism of cleavage in footprinting studies relies on hydroxyl radicals targeting exposed regions. Therefore, the more accessible a region is to the solvent, the higher the probability that it will be cleaved during the footprinting process.
04

Conclusion on Cleavage Likelihood

Given the principles of hydroxyl radical footprinting, regions with high solvent accessibility are more likely to experience cleavage. This can be used to map the exposed regions of an RNA, DNA, or protein structure.

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Key Concepts

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

Solvent Accessibility
Solvent accessibility is an important concept when analyzing the susceptibility of DNA or proteins to chemical modifications.
It refers to the extent to which molecules, such as those that make up DNA or proteins, are exposed to their surrounding environment.
In biochemical contexts, this environment is usually an aqueous solution.
  • Highly solvent-accessible regions are those parts of molecules that interact actively with water or other solvents.
  • Buried or protected regions are less exposed and generally more shielded within the molecular structure.
Understanding this concept is crucial in experiments like hydroxyl radical footprinting, where areas with greater solvent accessibility are more likely to undergo cleavage as they are more exposed to reactive species.
Cleavage Mechanism
The cleavage mechanism in hydroxyl radical footprinting provides insight into how molecules interact with their environment.
In this method, hydroxyl radicals serve as the cleaving agents, especially targeting parts of molecules that are solvent-exposed.
  • Hydroxyl radicals are highly reactive and can break chemical bonds within molecular structures.
  • In the context of footprinting, these radicals help identify the solvent-accessible regions by cleaving them more readily than the sheltered areas.
The cleavage occurs because these radicals seek available targets to react with, making areas that are solvent-accessible most susceptible.
This mechanism allows researchers to explore the dynamic aspects of molecular structures, such as protein folding or DNA configuration at their exposed sites.
DNA Structure Analysis
DNA structure analysis is enriched by using techniques such as hydroxyl radical footprinting.
Scientists can determine which parts of the DNA strands are exposed to solvents and which are protected. This adds essential details about the double helix conformation and flexibility.
  • The regions that get cleaved indicate exposure and suggest points of interaction with the environment or proteins.
  • Knowledge about which sites are solvent-accessible can help in identifying functional areas like binding sites or areas involved in regulation.
DNA footprinting thus provides a map of structurally significant components that influence the DNA's behavior in biological processes.
Protein Structure Mapping
Protein structure mapping through hydroxyl radical footprinting enables a deeper understanding of protein organization and function.
The technique helps chart which portions of a protein are solvent-accessible, offering clues on how proteins might interact within cells or with other molecules.
  • Information gathered can reveal active sites, areas involved in catalysis, or segments critical for protein stability.
  • Cleavage patterns suggest which regions are likely interacting with the solvent, indicating flexibility or conformation changes.
This approach provides a snapshot of the protein's functional zones, helping in the study of protein dynamics, interactions, and structural changes.

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Most popular questions from this chapter

Which of the following effects favors RNA folding? a. Interactions between phosphate groups. b. Kinetic traps of altemative structures. c. Neutralization of backbone charge by counterions. d. The entropy of the native state compared to the unfolded state.

A solution \(x\)-ray scattering experiment for a protein is performed in increasing amounts of urea. The data show a difference in the radius of gyration at \(6 \mathrm{M}\) urea and \(0.1 \mathrm{M}\) urea. a. Why is the radius of gyration different between an unfolded and folded protein even though both contain the same number of residues? b. How will the measured radius of gyration depend on the concentration of urea?

A mutation of core residues in the E. coli protein Rop speeds up the rate of protein folding from \(0.013 \mathrm{sec}^{-1}\) to \(1.3 \mathrm{sec}^{-1}\). a. What is the effect of the mutation on the free energy of the transition state relative to the unfolded state? b. Given that a simple mutation can increase the folding rate, what does this result suggest about the relationship between the protein folding rate and natural selection? (Data based on M. Munson, K.S. Anderson, and L. Regan, Structure: Folding and Design, 2: 77-87, 1997.)

Which of the following is least likely to lead to RNA unfolding? a. Increasing \(\left.\mid \mathrm{Mg}^{2+}\right]\) by \(1 \mathrm{mM}\). b. Increasing the temperature to \(75^{\circ} \mathrm{C}\). c. Adding \(1 \mathrm{M}\) EDTA. d. Adding \(6 \mathrm{M}\) urea.

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