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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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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.
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Thermal Energy Microscopically, thermal energy is the kinetic energy associated with the random motion of atoms and molecules. Temperature is a quantitative measure of “hot” or “cold”, which depends on the amount of thermal energy. When the atoms and molecules in an object are moving or vibrating quickly, they have a higher average kinetic energy (KE) (or higher thermal energy), and the object is perceived as “hot”, or it is described as being at a...
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When a substance—isolated from its environment—is subjected to heat changes, corresponding changes in temperature and phase of the substance is observed; this is graphically represented by heating and cooling curves.
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Heat Capacities of an Ideal Gas II01:23

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For a system that undergoes a thermodynamic process at a constant volume condition, the heat absorbed is used only to increase the system's internal energy and not for doing any kind of work. While for a system undergoing a thermodynamic process under a constant pressure condition, the amount of heat absorbed is used not only for increasing the internal energy (as a function of temperature) but also for doing some work. The molar heat capacity is the amount of heat required to increase the...
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Protein Folding

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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
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Heat Capacity: Problem-Solving01:17

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The heat capacity of a gas is the amount of heat energy required to raise the temperature of a unit mass of gas by one degree Celsius. It is an important thermodynamic property of gases, and its determination is essential in many industrial and scientific applications. Here are the steps to solve problems related to the heat capacities of gases:
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Related Experiment Video

Updated: Jul 20, 2025

Single-molecule Manipulation of G-quadruplexes by Magnetic Tweezers
08:28

Single-molecule Manipulation of G-quadruplexes by Magnetic Tweezers

Published on: September 19, 2017

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Heat capacity changes associated with G-quadruplex unfolding.

Arees Garabet1, Lutan Liu1, Tigran V Chalikian1

  • 1Department of Pharmaceutical Sciences, Leslie Dan Faculty of Pharmacy, University of Toronto, 144 College Street, Toronto, Ontario M5S 3M2, Canada.

The Journal of Chemical Physics
|August 1, 2023
PubMed
Summary
This summary is machine-generated.

This study directly measured the heat capacity changes (ΔCP) during G-quadruplex unfolding, revealing its crucial role in thermodynamic stability. Neglecting ΔCP can lead to significant errors in understanding G-quadruplex thermodynamics.

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Last Updated: Jul 20, 2025

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

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Thermodynamics

Background:

  • G-quadruplexes are four-stranded DNA structures involved in genomic regulation.
  • Thermodynamic stability (ΔG) of G-quadruplexes is key to understanding their function.
  • Differential heat capacity (ΔCP) is vital for describing temperature-dependent thermodynamic properties but has not been directly measured for G-quadruplex unfolding.

Purpose of the Study:

  • To directly measure the change in heat capacity (ΔCP) during the unfolding of G-quadruplexes.
  • To assess the impact of ΔCP on thermodynamic parameters (ΔH, ΔS, ΔG) of G-quadruplexes.
  • To highlight the importance of considering ΔCP in conformational studies of guanine-rich DNA.

Main Methods:

  • Differential scanning calorimetry (DSC) was employed to measure ΔCP.
  • G-quadruplexes were formed from modified DNA sequences of c-MYC, VEGF, and Bcl-2 oncogene promoter regions.

Main Results:

  • The average ΔCP for G-quadruplex unfolding was determined to be 0.49 ± 0.12 kcal mol⁻¹ K⁻¹.
  • Disregarding ΔCP introduced substantial errors in extrapolated ΔH and ΔS values.
  • Neglecting ΔCP can result in up to 140% relative error in ΔG extrapolated to room temperature.

Conclusions:

  • Direct measurement of ΔCP is essential for accurate thermodynamic characterization of G-quadruplexes.
  • Accurate thermodynamic data, including ΔCP, is critical for understanding the role of G-quadruplexes in genomic events.
  • The study underscores the necessity of incorporating ΔCP into conformational analyses of G-rich DNA structures.