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 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.
D001426:Bacterial Proteins / Q000737:chemistry; D004722:Endoribonucleases / Q000737:chemistry*; D004795:Enzyme Stability; D011485:Protein Binding; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry*; D012260:Ribonucleases / Q000037:antagonists & inhibitors / Q000737:chemistry*; D013816:Thermodynamics
D001426:Bacterial Proteins; D011506:Proteins; C057438:barstar protein, Bacillus amyloliquefaciens; D004722:Endoribonucleases; D012260:Ribonucleases; C019760:Bacillus amyloliquefaciens ribonuclease; C022543:ribonuclease T(2)