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Protein Folding

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Related Experiment Video

Updated: Jun 13, 2025

Single-molecule Manipulation of G-quadruplexes by Magnetic Tweezers

Single-molecule Manipulation of G-quadruplexes by Magnetic Tweezers

Published on: September 19, 2017

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.

Biorxiv : the Preprint Server for Biology

|September 16, 2024

Summary

This summary is machine-generated.

A rapid collapse, like protein molten globule formation, precedes G-quadruplex folding. This early step in oligonucleotide G4 folding occurs in under 600 ms.

Keywords:

G-quadruplex Telomere folding Time-resolved SAXS

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Area of Science:

Biophysics
Structural Biology
Molecular Biology

Background:

G-quadruplex (G4) structures are crucial in telomere maintenance and gene regulation.
Understanding the folding pathways of G-quadruplexes is key to elucidating their biological functions.

Purpose of the Study:

To investigate the early folding dynamics of hybrid 1 and hybrid 2 telomeric G-quadruplex structures.
To characterize the rapid structural changes during G4 formation using time-resolved experiments.

Main Methods:

Time-resolved small-angle X-ray scattering (TR-SAXS) to monitor structural changes in real-time.
pH-jump kinetic studies to initiate and track folding.
SAXS Ensemble Optimization Method (EOM) for modeling the unfolded state.

Main Results:

A rapid, monophasic collapse of unfolded oligonucleotides was observed, completing in <600 ms.
The radius of gyration decreased from 20.6 to 12.6 Å during this collapse.
SAXS EOM analysis revealed the unfolded state as a dynamic ensemble with transient hairpin structures.
Equilibrium studies confirmed complete G4 unfolding at alkaline pH, but not in LiCl.

Conclusions:

G-quadruplex folding involves an initial rapid collapse, analogous to molten globule formation in proteins.
This collapse is followed by a conformational search leading to the formation of native G4 contacts.
The findings provide new insights into the G4 folding pathway and the nature of the unfolded state.