Title of article
Thermodynamics of denaturation of complexes of barnase and binase with barstar Original Research Article
Author/Authors
Vladimir A. Mitkevich، نويسنده , , Alexey A. Schulga، نويسنده , , Yaroslav S. Ermolyuk، نويسنده , , Vladimir M. Lobachov، نويسنده , , Vladimir O. Chekhov، نويسنده , , Gennady I. Yakovlev، نويسنده , , Robert W. Hartley، نويسنده , , C. Nick Pace، نويسنده , , Mikhail P. Kirpichnikov، نويسنده , , Alexander A. Makarov، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2003
Pages
8
From page
383
To page
390
Abstract
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.
Keywords
thermal stability , electrostatic interactions , Barnase , Binase , Barstar , Protein–protein complex
Journal title
Biophysical Chemistry
Serial Year
2003
Journal title
Biophysical Chemistry
Record number
1113326
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