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Related Concept Videos

Protein Folding01:25

Protein Folding

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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
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Molecular Chaperones and Protein Folding03:00

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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.
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Updated: May 30, 2025

Single-molecule Manipulation of G-quadruplexes by Magnetic Tweezers
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Early events in G-quadruplex folding captured by time-resolved small-angle X-ray scattering.

Robert C Monsen1, T Michael Sabo1, Robert Gray1

  • 1Department of Medicine, UofL Health Brown Cancer Center, University of Louisville, Louisville KY, 505 S Hancock St, Louisville, KY 40202, United States.

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Summary

A rapid collapse, similar to protein molten globule formation, is a key early step in G-quadruplex (G4) folding. This collapse occurs within milliseconds, preceding slower folding events.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • G-quadruplexes (G4) are crucial nucleic acid structures with diverse biological roles.
  • Understanding G4 folding pathways is essential for elucidating their function.
  • Previous models lacked detailed insights into the initial folding dynamics.

Purpose of the Study:

  • To investigate the early folding events of hybrid 1 and hybrid 2 telomeric G-quadruplexes.
  • To quantify the kinetics and structural changes during G4 folding.
  • To characterize the unfolded state of G-quadruplexes.

Main Methods:

  • Time-resolved small-angle X-ray scattering (SAXS) experiments.
  • pH-jump initiation of folding.
  • Hand-mixing kinetic studies.
  • SAXS Ensemble Optimization Method (SAXS-EOM).

Main Results:

  • A rapid, monophasic collapse of unfolded G-quadruplexes was observed within 600 ms.
  • The collapse significantly reduced the radius of gyration, indicative of compacting.
  • The unfolded state exists as a dynamic ensemble of flexible chains with transient hairpins.
  • G4 unfolding is complete at alkaline pH but not in LiCl solutions.

Conclusions:

  • G-quadruplex folding initiates with a rapid collapse, analogous to molten globule formation in proteins.
  • Subsequent slower steps involve conformational searching within the collapsed structure.
  • The unfolded state is not a random coil but a dynamic ensemble.
  • Established G4 unfolding conditions require re-evaluation.