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 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.
Wintrode
P L
PL
Department of Biology, Johns Hopkins University, Baltimore, Maryland 21218.
Makhatadze
G I
GI
Privalov
P L
PL
D002151:Calorimetry; D006358:Hot Temperature; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D008956:Models, Chemical; D011487:Protein Conformation; D012996:Solutions; D013816:Thermodynamics; D014452:Ubiquitins / Q000737:chemistry*; D014867:Water
D012996:Solutions; D014452:Ubiquitins; D014867:Water