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Microcalorimetry of biological macromolecules

Authors
Journal
Biophysical Chemistry
0301-4622
Publisher
Elsevier
Publication Date
Volume
126
Identifiers
DOI: 10.1016/j.bpc.2006.05.004
Keywords
  • Microcalorimetry
  • Thermodynamics
  • Proteins
  • Dna
  • Unfolding
  • Association
  • Hydration
Disciplines
  • Biology
  • Physics

Abstract

Abstract 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.

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