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Related Experiment Video

Updated: Mar 12, 2026

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
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Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen

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Micro-differential scanning calorimeter for liquid biological samples.

Shuyu Wang1, Shifeng Yu2, Michael S Siedler3

  • 1Department of Mechanical Engineering, Stony Brook University, Stony Brook, New York 11794, USA.

The Review of Scientific Instruments
|November 3, 2016
PubMed
Summary

We created a sensitive micro-differential scanning calorimeter (DSC) for protein analysis. This compact device uses microfluidics and advanced sensors for precise, low-volume measurements, enabling high-throughput biochemical assays.

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Related Experiment Videos

Last Updated: Mar 12, 2026

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A Package of Established Analytical Tools to Investigate the Solid-State Alteration of Lipid-Based Excipients
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Area of Science:

  • Biophysical Chemistry
  • Analytical Chemistry
  • Materials Science

Background:

  • Accurate characterization of liquid protein samples is crucial for biochemical and pharmaceutical applications.
  • Existing methods for protein thermal analysis often require larger sample volumes and specialized equipment.
  • There is a need for sensitive, miniaturized analytical tools for efficient protein sample evaluation.

Purpose of the Study:

  • To develop and validate an ultrasensitive micro-differential scanning calorimeter (DSC) for liquid protein sample characterization.
  • To integrate microfluidics, vanadium oxide thermistors, and flexible polymer substrates for enhanced sensor performance.
  • To demonstrate the device's capability in analyzing protein unfolding thermodynamics.

Main Methods:

  • Fabrication of a microfluidic chip incorporating vanadium oxide thermistors on flexible polymer substrates.
  • Integration of microfluidic chambers for precise control of liquid sample volumes (1 μl).
  • Characterization of sensor performance, including sensitivity (6 V/W), thermal conductivity (0.7 mW/K), and power resolution (40 nW).

Main Results:

  • The developed micro-DSC sensor exhibited high sensitivity, low thermal conductivity, and high power resolution.
  • The device successfully measured the thermal unfolding of lysozyme.
  • Obtained transition temperature and enthalpy change values were consistent with established literature data.

Conclusions:

  • The ultrasensitive micro-DSC offers a compact, cost-effective solution for liquid protein characterization.
  • The sensor's performance indicates its potential for high-throughput biochemical measurements.
  • Parallel operation with miniaturized sample consumption can significantly enhance analytical efficiency.