ArticleNucleic acids research2025
Early events in G-quadruplex folding captured by time-resolved small-angle X-ray scattering.
Article in Nucleic acids research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed.
- Ultrafast time-resolved small-angle X-ray scattering setup on the FemtoMAX beamline.Journal of synchrotron radiation · 2026Article
- Unraveling G-Quadruplex and i-Motif Coexistence Within a Double-Stranded DNA.Angewandte Chemie (International ed. in English) · 2026Article
- Sequence-Encoded Frustration Directs the Formation of Abridged G-Quadruplex Architectures.Angewandte Chemie (International ed. in English) · 2026Article
- Telomeric G-quadruplex intermediates unveiled by complex Markov network analysis.Scientific reports · 2026Article
- Auto-luminescence study of thermal unfolding of DNA G-quadruplexes.RSC advances · 2025Article
- RNA G-quadruplexes emerge from a compacted coil-like ensemble via multiple pathways.Nucleic acids research · 2025Article
- Crystal structures of distinct parallel and antiparallel DNA G-quadruplexes reveal structural polymorphism in C9orf72 G4C2 repeats.Nucleic acids research · 2025Article
- The structure, folding kinetics, and dynamics of long poly(UG) RNA.Nucleic acids research · 2025Article
- Advances in microfluidic mixers for time-resolved structural biology with X-rays.Biophysical reviews · 2025Review
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Abstract
Time-resolved small-angle X-ray experiments are reported here that capture and quantify a previously unknown rapid collapse of the unfolded oligonucleotide as an early step in the folding of hybrid 1 and hybrid 2 telomeric G-quadruplex structures. The rapid collapse, initiated by a pH jump, is characterized by an exponential decrease in the radius of gyration from 24.3 to 12.6 Å. The collapse is monophasic and is complete in <600 ms. Additional hand-mixing pH-jump kinetic studies show that slower kinetic steps follow the collapse. The folded and unfolded states at equilibrium were further characterized by SAXS studies and other biophysical tools, showing that G4 unfolding was complete at alkaline pH, but not in LiCl solution as is often claimed. The SAXS Ensemble Optimization Method analysis reveals models of the unfolded state as a dynamic ensemble of flexible oligonucleotide chains with a variety of transient hairpin structures. These results suggest a G4 folding pathway in which a rapid collapse, analogous to molten globule formation seen in proteins, is followed by a confined conformational search within the collapsed particle to form the native contacts ultimately found in the stable folded form.
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