AI Article Synopsis
- The study used differential scanning calorimetry to analyze how protein complexes, specifically barnase, binase, and their inhibitor barstar, denature thermodynamically with varying free energy from -8 to -16 kcal/mol.
- The research focused on both the wild-type proteins and their mutant versions, exploring the stability of these protein complexes during thermal unfolding.
- Results supported the existing thermodynamics model by Brandts and Lin, which is designed for studying tight protein complexes that exhibit two-state thermal unfolding behavior.
Article 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.
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| http://dx.doi.org/10.1016/s0301-4622(03)00103-0 | DOI Listing |
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