Dynamic analysis of differential scanning calorimetry data

• Published in: Biophysical chemistry Vol. 27; no. 1; pp. 87 - 96
• Main Authors: Mayorga, Obdulio Lopez, Freire, Ernesto
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.07.1987
• Subjects: 1,2-Dipalmitoylphosphatidylcholine; Calorimetry - methods; Calorimetry, Differential Scanning - methods; Dipalmitoylphosphatidylcholine; DSC; Dynamic deconvolution; Heat capacity; Kinetics; Lipid Bilayers; Mathematics; Models, Biological; Ribonuclease A; Ribonuclease A; Heat capacity; Dynamic deconvolution; Kinetics; DSC; Dipalmitoylphosphatidylcholine
• ISSN: 0301-4622; 1873-4200
• DOI: 10.1016/0301-4622(87)80049-2

The apparent heat capacity function measured by high-sensitivity differential scanning calorimetry contains dynamic components of two different origins: (1) an intrinsic component arising from the finite instrument time response; and (2) a sample component arising from the kinetics of the thermal transition under study. The intrinsic instrumental component is always present and its effect on the shape of the experimental curve depends on the magnitude of the calorimeter response time. Usually, high-sensitivity instruments exhibit characteristic time constants varying from 10 to 100 s. This slow response introduces distortions in the shape of the heat capacity function especially at fast scanning rates. In addition to this instrumental component, dynamic effects due to sample relaxation processes also contribute to the shape of the experimental heat capacity profile. Since the nature and magnitude of these effects are a function of the kinetic parameters of the transition, they can be used to obtain kinetic information. This communication presents a dynamic deconvolution technique directed to remove artificial distortions in the shape of the heat capacity function measured at any scanning rate, and to obtain a kinetic characterization of a thermally induced transition. The kinetic characterization obtained by this method allows the researcher to obtain transition relaxation times as a continuous function of temperature. This technique has been applied to the thermal unfolding of ribonuclease A and the pretransition of dipalmitoylphosphatidylcholine (DPPC). In both systems the transition relaxation times are temperature dependent. For the protein system the relaxation time is very slow below the transition temperature ( 3&#x0303;0 s) and very fast above T m( < 1 s) in agreement with direct kinetic measurements. For the pretransition of DPPC, the relaxation time is maximal at the transition midpoint and of the order of approx. 40 s.