Thermodynamics of denaturation of complexes of barnase and binase with barstar

Thermodynamics of denaturation of complexes of barnase and binase with barstar

Differential scanning calorimetry was used to study the thermodynamics of denaturation of protein complexes for which the free energy stabilizing the complexes varied between −8 and −16 kcal/mol. The proteins studied were the ribonucleases barnase and binase, their inhibitor barstar and mutants ther...

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Veröffentlicht in:Biophysical chemistry 2003-09, Vol.105 (2), p.383-390
Hauptverfasser: Mitkevich, Vladimir A., Schulga, Alexey A., Ermolyuk, Yaroslav S., Lobachov, Vladimir M., Chekhov, Vladimir O., Yakovlev, Gennady I., Hartley, Robert W., Nick Pace, C., Kirpichnikov, Mikhail P., Makarov, Alexander A.
Format: Artikel
Sprache:eng
Schlagworte:
Bacterial Proteins - chemistry
Barnase
Barstar
Binase
Electrostatic interactions
Endoribonucleases - chemistry
Enzyme Stability
Protein Binding
Protein Denaturation
Proteins - chemistry
Protein–protein complex
Ribonucleases - antagonists & inhibitors
Ribonucleases - chemistry
Thermal stability
Thermodynamics
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Zusammenfassung:Differential scanning calorimetry was used to study the thermodynamics of denaturation of protein complexes for which the free energy stabilizing the complexes varied between −8 and −16 kcal/mol. The proteins studied were the ribonucleases barnase and binase, their inhibitor barstar and mutants thereof, and complexes between the two. The results are in good agreement with the model developed by Brandts and Lin for studying the thermodynamics of denaturation for tight complexes between two proteins which undergo two-state thermal unfolding transitions.
ISSN:0301-4622
1873-4200
DOI:10.1016/S0301-4622(03)00103-0