Abstract
Recent developments of differential adiabatic scanning microcalorimetry have been permitted the precise measurements of the slight changes in heat capacity of the dilute protein solution which is caused by the transition of the higher order protein structure. As the most important feature of the calorimetry is the direct observation of thermodynamic functions, it is an effective measurement for the thermal stability and fluctuation of protein molecule. In this article, a brief review on the basic principle of the calorimetry and new statistical thermodynamic methods for the calorimetry data analysis, by which thermodynamic characteristics of globular proteins have been well recognized, is presented. Cold denaturation and multistate transition of protein molecule are mentioned.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
