Comparison of transition states obtained upon modeling of unfolding of immunoglobulin-binding domains of proteins L and G caused by external action with transition states obtained in the absence of force probed by experiments.
We have studied the extent of coincidence of the pathway of unfolding of protein globules upon experimental modeling of protein unfolding caused by external actions and denaturants. To this end, we compared experimental Phi-values reported in the literature and Phi-values obtained by us upon modeling of unfolding of immunoglobulin-binding domains of proteins L and G caused by external actions at a constant rate. A comparison of the results of calculation with the experimental data shows that the folding pathways for protein L coincide, while those for protein G do not coincide despite structural similarity of these proteins.
Glyakina
A V
AV
Institute of Mathematical Problems of Biology, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia.
Balabaev
N K
NK
Galzitskaya
O V
OV
D000465:Algorithms; D001665:Binding Sites; D007136:Immunoglobulins / Q000378:metabolism*; D007700:Kinetics; D008958:Models, Molecular; D009154:Mutation; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D013816:Thermodynamics
D007136:Immunoglobulins; D011506:Proteins