Related Experiment Video
Updated: Aug 29, 2025

Application of Stopped-flow Kinetics Methods to Investigate the Mechanism of Action of a DNA Repair Protein
Published on: March 31, 2010
The incipient denaturation mechanism of DNA
Min Xu1, Tinghui Dai1, Yanwei Wang1
1Department of Physics, Wenzhou University Wenzhou 325035 China minxu526@foxmail.com wangyw@wzu.edu.cn yanggc@wzu.edu.cn +86-577-8668-9010 +86-577-8668-9033.
Abstract:
DNA denaturation is related to many important biological phenomena, such as its replication, transcription and the interaction with some specific proteins for single-stranded DNA. Dimethyl sulfoxide (DMSO) is a common chemical agent for DNA denaturation. In the present study, we investigate quantitatively the effects of different concentrations of DMSO on plasmid and linear DNA denaturation by atomic force microscopy (AFM) and UV spectrophotometry. We found that persistent length of DNA decreases significantly by adding a small amount of DMSO before ensemble DNA denaturation occurs; the persistence length of DNA in 3% DMSO solution decreases to 12 nm from about 50 nm without DMSO in solution. And local DNA denaturation occurs even at very low DMSO concentration (such as 0.1%), which can be directly observed in AFM imaging. Meanwhile, we observed the forming process of DNA contacts between different parts for plasmid DNA with increasing DMSO concentration. We suggest the initial mechanism of DNA denaturation as follows: DNA becomes more flexible due to the partial hydrogen bond braking in the presence of DMSO before local separation of the two complementary nucleotide chains.
Related Concept Videos
Protein Denaturation
Single-Strand DNA Binding Proteins
Overview of DNA Repair
Chemically...
Spontaneous and Induced Mutations
The DNA Replication Fork
The DNA Helix

