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Related Experiment Videos

Cold destabilisation of enzymes.

R H Hatley1, F Franks

  • 1Pafra Ltd., Biopreservation Division, Cambridge, UK.

Faraday Discussions
|January 1, 1992
PubMed
Summary

This study reveals chymotrypsinogen exhibits cold instability, with its heat capacity decreasing at lower temperatures. This provides a more reliable thermodynamic stability profile than previous research.

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Area of Science:

  • Biochemistry
  • Physical Chemistry
  • Protein Science

Background:

  • Proteins exhibit complex thermal stability profiles.
  • Cold instability is a poorly understood phenomenon in protein thermodynamics.
  • Chymotrypsinogen serves as a model system for studying protein behavior.

Purpose of the Study:

  • To investigate the thermal stability profile of chymotrypsinogen.
  • To characterize the phenomenon of cold instability in proteins.
  • To construct a reliable thermodynamic stability profile for chymotrypsinogen.

Main Methods:

  • Differential scanning calorimetry (DSC) to measure heat capacities.
  • Spectrophotometry at ordinary temperatures.
  • Analysis of native and denatured protein states in undercooled solutions.

Main Results:

  • Partial heat capacities of both native and denatured chymotrypsinogen decrease with temperature.
  • A positive heat capacity difference (delta C) was observed in the accessible temperature range.
  • delta C is predicted to change sign at temperatures below experimental reach.

Conclusions:

  • The study provides a more reliable thermodynamic stability profile for chymotrypsinogen.
  • Findings highlight differences compared to other proteins studied only near denaturation temperatures.
  • Results align with theoretical predictions and low-temperature studies on lactate dehydrogenase.

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