Category Ranking

98%

Total Visits

921

Avg Visit Duration

2 minutes

Citations

20

Article Abstract

G-quadruplexes are special structures existing at the ends of human telomeres, the folding kinetics of which are essential for their functions, such as in the maintenance of genome stability and the protection of chromosome ends. In the present study, we investigated the folding kinetics of G-quadruplex in different monovalent cation environments and determined the detailed kinetic parameters for Na- and K-induced G-quadruplex folding, and for its structural transition from the basket-type Na form to the hybrid-type K form. More interestingly, although Li was often used in previous studies of G-quadruplex folding as a control ion supposed to have no effect, we have found that Li can actually influence the folding kinetics of both Na- and K-induced G-quadruplexes significantly and in different ways, by changing the folding fraction of Na-induced G-quadruplexes and greatly increasing the folding rates of K-induced G-quadruplexes. The present study may shed new light on the roles of monovalent cations in G-quadruplex folding and should be useful for further studies of the underlying folding mechanism.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5567087PMC
http://dx.doi.org/10.1042/BSR20170771DOI Listing

Publication Analysis

Top Keywords

folding kinetics
16
g-quadruplex folding
12
folding
10
monovalent cations
8
na- k-induced
8
k-induced g-quadruplexes
8
g-quadruplexes
5
effects monovalent
4
cations folding
4
kinetics
4

Similar Publications

Nucleic acid aptamers are artificial recognition elements with great potential in biotechnology. For their effective integration into nanodevices, rational strategies for optimizing aptamer affinity and regulating activity are essential. Artificial nucleotide analogs offer versatile tools for both fundamental and applied research in the aptamer field.

View Article and Find Full Text PDF

The energy landscape of folding in n-C14H30 described by a machine-learned potential.

J Chem Phys

September 2025

Yusuf Hamied Department of Chemistry. Lensfield Road, Cambridge CB2 1EW, United Kingdom.

Folding and unfolding in molecules as simple as short hydrocarbons and as complicated as large proteins continue to be an active research field. Here, we investigate folding in n-C14H30 using both density functional theory (DFT)/B3LYP calculations of 27 772 local minima and a kinetic transition network calculated for a previously reported potential energy surface (PES) obtained by fitting roughly 250 000 B3LYP energies. In addition to generating a database of minima and the transition states that connect them, these calculations and the PES based on them have been used to develop a simple and accurate model for the energy landscape.

View Article and Find Full Text PDF

Measurable neuromotor control deficits during functional task performance could provide objective criteria to aid in concussion diagnosis. However, many tools which measure these constructs are unidimensional and not clinically feasible. The purpose of this study was to assess the classification accuracy of a machine learning model using features measured by a clinically feasible movement-based assessment system (Mizzou Point-of-care Assessment System (MPASS) between athletes with and without concussion.

View Article and Find Full Text PDF

The divergence in folding pathways between RNA co-transcriptional folding (CTF) and free folding (FF) is crucial for understanding dynamic functional regulation of RNAs. Here, we developed a simplified all-atom molecular dynamics framework to systematically compare the folding kinetics of an RNA hairpin (PDB:1ZIH) under CTF and FF conditions. By analyzing over 800 microseconds of simulated trajectory, we found that despite convergence to identical native conformations across CTF simulations (with varied transcription rates) and FF simulations, they exhibit distinct preferences for the folding pathways defined by the order of base-pair formation.

View Article and Find Full Text PDF

The efficiency of enzymatic proteolysis is often attributed to the properties of the enzyme itself, with the substrate typically viewed as a passive participant. In this study, we demonstrate that the conformational state of the substrate critically influences proteolytic efficiency. Using human serum albumin (HSA) as a model substrate, papain as the enzyme, and urea as a controlled denaturing agent, we systematically investigated how substrate conformation might affect proteolysis.

View Article and Find Full Text PDF