G-quadruplex
G-quadruplex - Related Videos
11:25
A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1
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Cited by 6 •
2017
G4 Resolvase1 binds to G-quadruplex (G4) structures with the tightest reported affinity for a G4-binding protein and represents the majority of the G4-DNA unwinding activity in HeLa cells. We describe a novel protocol that harnesses the affinity and ATP-dependent unwinding activity of G4-Resolvase1 to specifically purify catalytically active recombinant G4R1.
08:28
Single-molecule Manipulation of G-quadruplexes by Magnetic Tweezers
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Cited by 4 •
2017
A single-molecule magnetic tweezers platform to manipulate G-quadruplexes is reported, which allows for the study of G4 stability and regulation by various proteins.
05:37
Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes
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2025
This protocol outlines a fluorescence microscopy-based single-molecule DNA replication assay, enabling real-time visualization of interactions between DNA polymerases and obstacles such as G-quadruplex structures.
03:38
Aptamer-Based Target Detection Facilitated by a 3-Stage G-Quadruplex Isothermal Exponential Amplification Reaction
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Cited by 1 •
2022
The present protocol demonstrates the use of a fast, 3-stage, aptamer-based exponential amplification assay to detect targets. Sample preparation, signal amplification, and color development are covered to implement this system to recognize the presence of theophylline over that of caffeine.
05:32
In Vitro Chemical Mapping of G-Quadruplex DNA Structures by Bis-3-Chloropiperidines
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2023
Bis-3-chloropiperidines (B-CePs) are useful chemical probes to identify and characterize G-quadruplex structures in DNA templates in vitro. This protocol details the procedure to perform probing reactions with B-CePs and to resolve reaction products by high-resolution polyacrylamide gel electrophoresis.
FAQs
The central monovalent cation helps organize and stabilize the stacked guanine tetrads. Potassium is identified as a common stabilizing ion within the core, so changing ionic conditions can shift the balance between folded and unfolded states. This dependence makes cation composition an important biochemical variable when interpreting G-quadruplex formation, persistence, or molecular recognition.
G-quadruplex folding is sensitive to more than the guanine-rich sequence. Ionic conditions can promote or disrupt the folded state, while interacting proteins can also influence whether the structure remains assembled. Because these factors act dynamically, observations made under one biochemical environment may not represent the same nucleic-acid state under another, an important consideration in molecular recognition studies.
Unlike conventional double-helix organization, G-quadruplexes add an alternative folding arrangement based on stacked guanine tetrads and Hoogsteen hydrogen bonding. Their ability to form and unfold dynamically means nucleic-acid structure is not fixed to a single architecture. This distinction helps explain why G4 analysis addresses higher-order folding and recognition rather than only conventional base pairing.
Researchers examine G-quadruplexes in telomeres, gene-regulatory regions, and RNA molecules because these settings connect structure with major biochemical questions. Telomere studies relate G4s to genome stability, whereas gene-regulatory and RNA studies help address effects on gene expression, nucleic-acid folding, and molecular recognition. The relevant context therefore depends on the biological process being investigated.
Structure-to-function analysis should link the G4 state with the biochemical setting in which it forms. Researchers can compare how sequence, ionic conditions, and interacting proteins affect folding or unfolding, then relate those changes to molecular recognition, genome stability, or gene expression. This approach keeps structural observations connected to potential consequences rather than treating the fold as static.
Interest in therapeutic design arises because G4 structures combine sequence-dependent folding with responsiveness to ionic conditions and interacting proteins. A design strategy can therefore treat the structure as a regulated molecular feature rather than an unchanging target. Studying these dependencies may help researchers consider how nucleic-acid organization, molecular recognition, and biological context should be incorporated into therapeutic concepts.