Differential Scanning Calorimetry
Differential Scanning Calorimetry - Related Videos
12:03
Differential Scanning Calorimetry
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2023
Source: Danielle N. Beatty and Taylor D. Sparks, Department of Materials Science and Engineering, The University of Utah, Salt Lake City, UT Differential scanning calorimetry (DSC) is an important measurement to characterize thermal properties of materials. DSC is used primarily to calculate the amount of heat stored in a material as it heats up (heat capacity) as well as the heat absorbed or released during chemical reactions or phase changes. However, measurement of this heat can also lead to...
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Using Differential Scanning Calorimetry to Measure Changes in Enthalpy
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2023
Source: Laboratory of Dr. Terry Tritt — Clemson University Differential Scanning Calorimetry (DSC) is a method of thermodynamic analysis based on heat-flux method, wherein a sample material (enclosed in a pan) and an empty reference pan are subjected to identical temperature conditions. The energy difference that is required to maintain both the pans at the same temperature, owing to the difference in the heat capacities of the sample and the reference pan, is recorded as a function of...
08:13
Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
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Cited by 117 •
2017
Differential scanning calorimetry measures the thermal transition temperature(s) and total heat energy required to denature a protein. Results obtained are used to assess the thermal stability of protein antigens in vaccine formulations.
07:16
Differential Scanning Calorimetry to Study DNA Aptamer-Thermolabile Ligand Interaction
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2025
This video demonstrates differential scanning calorimetry — a technique to study the interaction between a biomolecule and a ligand. The binding of a DNA aptamer and a thermolabile ligand is studied by applying repeated heating and cooling cycles to the sample and obtaining scans for thermodynamic analysis.
03:02
Constant Pressure Calorimetry
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2020
Calorimetry is a technique used to measure the amount of heat involved in a chemical or physical process or to measure the heat transferred to or from a substance. The heat is exchanged with a calibrated and insulated device called the calorimeter. Calorimetry experiments are based on the assumption that there is no heat exchange between the insulated calorimeter and the external environment. The well-insulated calorimeters prevent the transfer of heat between the calorimeter and its external...
FAQs
During a controlled scan, the instrument compares the energy needed to keep the biological sample and reference at the same temperature. A greater or lesser heat requirement produces a heat-flow signal that can be interpreted as endothermic or exothermic. This distinction helps associate observed events with processes such as protein unfolding, melting, or crystallization.
Heating and cooling expose different thermal events within the same analytical framework. A heating scan can reveal events such as protein unfolding or melting, whereas cooling can identify events including crystallization. Examining these transitions provides a broader picture of how a biological material responds as temperature changes in opposite directions.
It can compare the thermal behavior of a protein under different conditions to characterize ligand-induced changes. Because the measurement tracks energy associated with thermal transitions, differences in the resulting heat-flow behavior provide quantitative information about how ligand presence relates to protein stability and molecular interactions. This makes DSC useful for biochemical characterization.
Thermal transitions serve as measurable indicators of changes in molecular state. For proteins, unfolding is a detectable transition; for lipid membranes, phase transitions report changes in membrane organization; and for nucleic acids, the thermal response helps characterize their behavior. DSC therefore connects heat-flow events with structural properties across biological materials.
An experiment requires a biological sample, a reference, and a controlled temperature program. The instrument maintains both at the same temperature while recording their difference in energy requirement during heating or cooling. This arrangement allows the measured signal to reflect thermal behavior associated with the sample rather than simply the temperature program itself.
Within biology, DSC can be applied to proteins, lipid membranes, and nucleic acids. It helps characterize protein stability, ligand-induced changes, membrane phase transitions, and nucleic acid behavior. The same technique therefore supports questions about molecular structure and interactions as well as the thermal properties of different classes of biological material.
Measurements can provide quantitative insight into formulation stability, making DSC relevant to biopharmaceutical development. Researchers can examine thermal behavior alongside protein stability and ligand-induced changes to characterize how a formulation relates to molecular properties. The resulting information supports biochemical research and helps assess stability-related questions during development.