TY - JOUR
T1 - Calorimetry
T2 - A tool for DNA and ligand—DNA studies
AU - Breslauer, Kenneth J.
AU - Freire, Ernesto
AU - Straume, Martin
N1 - Funding Information:
This work was supported by grants from the National Institutes of Health: GM23509 (K.J.B.), GM34469 (K.J.B.), CA47795 (K.J.B.), RR04328 (E.F.), NS24520 (E.F.), and GM37911 (E.F.).
PY - 1992/1/1
Y1 - 1992/1/1
N2 - This chapter discusses the unique information that can be obtained by the application of selected calorimetric techniques to the study of DNA. The chapter demonstrates calorimetry to be a powerful tool in biophysical research, capable of uniquely providing thermodynamic and extrathermodynamic characterizations of DNA structure, conformational transitions, and ligand interactions. A differential scanning calorimeter is an instrument that allows to measure continuously the heat capacity of a system as a function of temperature. Isothermal mixing calorimetry has been used in nucleic acid studies to characterize the influence of metal ion binding; to determine the enthalpy of duplex formation from the mixing of two complementary strands; to measure the energetics of pH-induced changes in nucleic acid structure; and to determine the enthalpy of small ligand-DNA interactions and protein–DNA interactions. Multifrequency calorimetry has been applied to the analysis of membrane phase transitions and to the folding–unfolding transition of the protein cytochrome c.
AB - This chapter discusses the unique information that can be obtained by the application of selected calorimetric techniques to the study of DNA. The chapter demonstrates calorimetry to be a powerful tool in biophysical research, capable of uniquely providing thermodynamic and extrathermodynamic characterizations of DNA structure, conformational transitions, and ligand interactions. A differential scanning calorimeter is an instrument that allows to measure continuously the heat capacity of a system as a function of temperature. Isothermal mixing calorimetry has been used in nucleic acid studies to characterize the influence of metal ion binding; to determine the enthalpy of duplex formation from the mixing of two complementary strands; to measure the energetics of pH-induced changes in nucleic acid structure; and to determine the enthalpy of small ligand-DNA interactions and protein–DNA interactions. Multifrequency calorimetry has been applied to the analysis of membrane phase transitions and to the folding–unfolding transition of the protein cytochrome c.
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U2 - 10.1016/0076-6879(92)11030-M
DO - 10.1016/0076-6879(92)11030-M
M3 - Article
C2 - 1406326
AN - SCOPUS:0026687954
SN - 0076-6879
VL - 211
SP - 533
EP - 567
JO - Methods in enzymology
JF - Methods in enzymology
IS - C
ER -