Study of pH-induced folding and unfolding kinetics of the DNA i-motif by stopped-flow circular dichroism.

Langmuir

Key Laboratory of Organic Optoelectronics & Molecular Engineering of the Ministry of Education, Department of Chemistry, Tsinghua University, Beijing 100084, China.

Published: December 2012

Using the stopped-flow circular dichroism (SFCD) technique, we investigate the kinetics of the pH-induced folding and unfolding process of the DNA i-motif. The results show that the molecule can fold or unfold on a time scale of 100 ms when the solution pH is changed. It is also found that the folding and unfolding rates strongly depend on the solution pH. On the basis of quantitative data, we propose theoretical models to decipher the folding and unfolding kinetics. Our models suggest that the cooperativity of protons is crucial for both the folding and unfolding process. In the unfolding process, the cooperative neutralization of two protons (out of the total six protons in the i-motif molecule) is the only rate-limiting step. In the folding process, there exists a critical step in which three protons bind cooperatively to the DNA strand. These results offer an in-depth understanding of the folding and unfolding kinetics of the DNA i-motif and may give precise guidance for constructing novel nanodevices based on the DNA i-motif.

Download full-text PDF

Source
http://dx.doi.org/10.1021/la303851aDOI Listing

Publication Analysis

Top Keywords

folding unfolding
24
dna i-motif
16
unfolding kinetics
12
unfolding process
12
ph-induced folding
8
kinetics dna
8
stopped-flow circular
8
circular dichroism
8
i-motif molecule
8
folding
7

Similar Publications

Bone lengthening and fracture repair depend on the anabolic properties of chondrocytes that function in an avascular milieu. The limited supply of oxygen and nutrients calls into question how biosynthesis and redox homeostasis are guaranteed. Here we show that glucose metabolism by the pentose phosphate pathway (PPP) is essential for endochondral ossification.

View Article and Find Full Text PDF

The pseudogap phenomena have been a long-standing mystery of the cuprate high-temperature superconductors. The pseudogap in the electron-doped cuprates has been attributed to band folding due to antiferromagnetic (AFM) long-range order or short-range correlation. We performed an angle-resolved photoemission spectroscopy study of the electron-doped cuprates PrLaCeCuO showing spin-glass, disordered AFM behaviors, and superconductivity at low temperatures and, by measurements with fine momentum cuts, found that the gap opens on the unfolded Fermi surface rather than the AFM Brillouin zone boundary.

View Article and Find Full Text PDF

Kinetically controlled irreversible unfolding of esterase from Clostridium acetobutylicum: Thermal deactivation kinetics and structural studies.

Int J Biol Macromol

January 2025

Applied and Industrial Microbiology Laboratory, Department of Biotechnology, Bhupat and Jyoti Mehta School of Biosciences, Indian Institute of Technology, Madras, Chennai 600036, India. Electronic address:

This study involves the thermal characterization of Ca-Est, an esterase from Clostridium acetobutylicum which has been previously found to exhibit maximum specific activity at 60 °C. In the present study, Ca-Est showed maximum stability at 30 °C with almost 75 % of its initial activity being retained after incubation for 5 h and the stability decreased with increasing temperature. Analysis of the thermodynamic parameters revealed that the deactivation of Ca-Est is endothermic and enthalpically favored.

View Article and Find Full Text PDF

Efficient Cytosolic Delivery of Single-Chain Polymeric Artificial Enzymes for Intracellular Catalysis and Chemo-Dynamic Therapy.

J Am Chem Soc

January 2025

The State Key Laboratory of Molecular Engineering of Polymers and Department of Macromolecular Science, Fudan University, Shanghai 200438, P. R China.

Designing artificial enzymes for in vivo catalysis presents a great challenge due to biomacromolecule contamination, poor biodistribution, and insufficient substrate interaction. Herein, we developed single-chain polymeric nanoparticles with Cu/N-heterocyclic carbene active sites (SCNP-Cu) to function as peroxidase mimics for in vivo catalysis and chemo-dynamic therapy (CDT). Compared with the enzyme mimics based on unfolded linear polymer scaffold and multichain cross-linked scaffold, SCNP-Cu exhibits improved tumor accumulation and CDT efficiency both in vitro and in vivo.

View Article and Find Full Text PDF

Most conventional methods used to measure protein melting temperatures reflect changes in structure between different conformational states and are typically fit to a two-state model. Population abundances of distinct conformations were measured using variable-temperature electrospray ionization ion mobility mass spectrometry to investigate the thermally induced unfolding of the model protein cytochrome . Nineteen conformers formed at high temperature have elongated structures, consistent with unfolded forms of this protein.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!