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.

Abstract excerpt

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....

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