Microcalorimetry of biological macromolecules.
The capabilities of contemporary differential scanning and isothermal titration microcalorimetry for studying the thermodynamics of protein unfolding/refolding and their association with partners, particularly target DNA duplexes, are considered. It is shown that the predenaturational changes of proteins must not be ignored in studying the thermodynamics of formation of their native structure and their complexes with partners, particularly their cognate DNA duplexes.
Privalov
Peter L
PL
Johns Hopkins University, Baltimore, MD 21218, USA. privalov@jhu.edu
Dragan
Anatoly I
AI
D002151:Calorimetry / Q000379:methods*; D002152:Calorimetry, Differential Scanning / Q000379:methods*; D004247:DNA / Q000737:chemistry*; D006358:Hot Temperature; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
D011506:Proteins; D004247:DNA