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How it works
In DSC experiments, a sample is added to a cell or
container with a buffer, and the same buffer is placed
in a separate cell or container serving to be used as a
reference. Both the sample and reference are heated
and maintained at the same temperature throughout
the experiment. When the protein unfolds, it consumes
energy, which will reduce the temperature of its
container. This means more energy will be needed to
maintain the container's temperature. The enthalpy
(or the measurement of energy in a thermodynamic
system) of the unfolding process can be directly extracted
from the change of heat capacity or Cp with increasing
temperatures. From these data, one can also determine
the unfolding transition point, Tm.
Strengths
DSC is a label- and modification-free method that
measures a physical property of the system directly.
Weaknesses
DSC requires a large amount of sample and has a very low
throughput, so it may not be as helpful for laboratories that
need to measure the stability of many proteins at one time.
Conclusion
DSC is the gold standard for measuring thermal stability,
but its low throughput and high sample consumption rate
make it better suited to serve as a secondary step in the
workflow that occurs a er the initial screening if there is
an abundance of sample material to test. Because of its
drawbacks, DSC is rarely used for early drug discovery
screening.
Differential scanning calorimetry (DSC) is a thermoanalytical technique that measures the amount of heat that it takes to
increase the temperature of a sample molecule and a reference in solution.
Differential Scanning Calorimetry
