Thermodynamics of ubiquitin unfolding

The energetics of ubiquitin unfolding have been studied using differential scanning microcalorimetry. For the first time it has been shown directly that the enthalpy of protein unfolding is a nonlinear function of temperature. Thermodynamic parameters of ubiquitin unfolding were correlated with the...

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Veröffentlicht in:	Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 1994-03, Vol.18 (3), p.246-253
Hauptverfasser:	Wintrode, Patrick L., Makhatadze, George I., Privalov, Peter L.
Format:	Artikel
Sprache:	eng
Schlagworte:	Biological and medical sciences Calorimetry Conformational dynamics in molecular biology enthalpy Fundamental and applied biological sciences. Psychology heat capacity Hot Temperature Hydrogen Bonding Hydrogen-Ion Concentration microcalorimetry Models, Chemical Molecular biophysics Protein Conformation Solutions Thermodynamics Ubiquitins - chemistry Water
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Beschreibung
Zusammenfassung:	The energetics of ubiquitin unfolding have been studied using differential scanning microcalorimetry. For the first time it has been shown directly that the enthalpy of protein unfolding is a nonlinear function of temperature. Thermodynamic parameters of ubiquitin unfolding were correlated with the structure of the protein. The enthalpy of hydrogen bonding in ubiquitin was calculated and compared to that obtained for other proteins. It appears that the energy of hydrogen bonding correlates with the average length of the hydrogen bond in a given protein structure. © 1994 John Wiley & Sons, Inc.
ISSN:	0887-3585 1097-0134
DOI:	10.1002/prot.340180305