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Related Concept Videos

DNA as a Genetic Template02:05

DNA as a Genetic Template

Two structural features of the DNA molecule provide a basis for the mechanisms of heredity: the four nucleotide bases and its double-stranded nature. The Watson-Crick model of double-helical DNA structure, proposed in 1952, drew heavily upon the X-ray crystallography work of researchers Rosalind Franklin and Maurice Wilkins. Watson, Crick, and Wilkins jointly received the Nobel Prize in Physiology or Medicine for their work in 1962. Franklin was, controversially, excluded from the prize for...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
DNA Topoisomerases02:02

DNA Topoisomerases

Topoisomerases are enzymes that relax overwound DNA molecules during various cell processes, including DNA replication and transcription. These enzymes regulate positive and negative DNA supercoiling without changing the nucleotide sequence. DNA overwinding in a clockwise direction results in positively supercoiled DNA, whereas underwinding in a counterclockwise direction produces negatively supercoiled DNA.
Types and Mechanism of action
Topoisomerases are divided into two main types.  Type I...

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Related Experiment Video

Updated: May 21, 2026

Studying DNA Looping by Single-Molecule FRET
11:27

Studying DNA Looping by Single-Molecule FRET

Published on: June 28, 2014

Hydration changes upon DNA folding studied by osmotic stress experiments.

Shu-ichi Nakano1, Daisuke Yamaguchi, Hisae Tateishi-Karimata

  • 1Faculty of Frontiers of Innovative Research in Science and Technology, Konan University, Kobe, Japan. shuichi@center.konan-u.ac.jp

Biophysical Journal
|June 28, 2012
PubMed
Summary

Small molecules destabilize DNA structures, affecting their thermal stability. Water binding varies with DNA features, influencing hydration in non-aqueous systems.

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Related Experiment Videos

Last Updated: May 21, 2026

Studying DNA Looping by Single-Molecule FRET
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Estimation of Structural Sensitivity of Intrinsically Disordered Regions in Response to Hyperosmotic Stress in Living Cells Using FRET
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Measuring Biomolecular DSC Profiles with Thermolabile Ligands to Rapidly Characterize Folding and Binding Interactions
09:15

Measuring Biomolecular DSC Profiles with Thermolabile Ligands to Rapidly Characterize Folding and Binding Interactions

Published on: November 21, 2017

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Thermodynamics

Background:

  • Intracellular environments and osmotic stress alter nucleic acid thermal stability.
  • Understanding DNA structure thermodynamics in complex solutions is crucial.

Purpose of the Study:

  • To investigate the thermodynamic stability of DNA oligonucleotide structures.
  • To analyze the impact of neutral cosolutes and osmotic stress on DNA stability.
  • To elucidate the role of DNA hydration in different structural contexts.

Main Methods:

  • Thermodynamic analysis of DNA oligonucleotide structures.
  • Osmotic stress experiments.
  • Studies using basepair-mimic nucleosides and peptide nucleic acid.

Main Results:

  • Small cosolutes destabilize DNA basepair structures.
  • DNA structures with identical nearest-neighbor composition exhibit similar thermodynamic parameters across different cosolutes.
  • Water binding is minimal for flexible loops, unstable mismatches, and abasic sites, but significant for stable mismatch pairs.
  • The sugar-phosphate backbone and basepair conformation influence water binding to DNA.

Conclusions:

  • Cosolutes significantly impact DNA thermodynamic stability.
  • Water binding patterns reveal insights into DNA hydration.
  • Findings provide a basis for predicting nucleic acid behavior in non-aqueous systems.