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Related Concept Videos

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:22

Protein Folding

Overview
Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...

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Single-molecule Manipulation of G-quadruplexes by Magnetic Tweezers
08:28

Single-molecule Manipulation of G-quadruplexes by Magnetic Tweezers

Published on: September 19, 2017

Controlled-folding of a small molecule modulates DNA G-quadruplex recognition.

Sebastian Müller1, G Dan Pantoş, Raphaël Rodriguez

  • 1The University Chemical Laboratory, University of Cambridge, Cambridge, CB2 1EW, UK.

Chemical Communications (Cambridge, England)
|December 17, 2008
PubMed
Summary

Controlling small molecule folding allows for the differential recognition of various G-quadruplex structures. This finding advances the development of targeted G-quadruplex-binding agents.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Chemical Biology

Background:

  • G-quadruplexes are four-stranded nucleic acid structures with significant biological relevance.
  • Dysfunctional G-quadruplexes are implicated in various diseases, including cancer.
  • Targeting G-quadruplexes requires molecules with high specificity for distinct structural conformations.

Purpose of the Study:

  • To investigate the potential of a small molecule to differentially recognize diverse G-quadruplex (G4) structures.
  • To establish a method for controlling G4 recognition through small molecule folding modulation.

Main Methods:

  • Utilized spectroscopic techniques (e.g., UV-Vis, fluorescence) to monitor G4 folding and binding.
  • Employed biophysical methods to characterize the interaction between the small molecule and various G4 conformations.
  • Designed and synthesized a small molecule capable of adopting distinct folded states.

Main Results:

  • Demonstrated that the small molecule exhibits differential binding affinities towards different G-quadruplex topologies.
  • Showcased that modulating the folding of the small molecule is key to achieving selective G4 recognition.
  • Identified specific structural features of G-quadruplexes that are recognized by the folded small molecule.

Conclusions:

  • Small molecule folding control is a viable strategy for achieving differential recognition of G-quadruplex structures.
  • This approach offers a promising avenue for developing selective G-quadruplex-targeting therapeutics.
  • Further research into small molecule-G4 interactions could lead to novel diagnostic and therapeutic tools.