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Keywords:

  • domain swapping;
  • protein folding;
  • protein unfolding;
  • kinetics;
  • thermodynamics;
  • Cyanovirin-N;
  • SARS-CoV main protease;
  • thioredoxin

Abstract

The full or partial unfolding of proteins is widely believed to play an essential role in three-dimensional domain swapping. However, there is little research that has rigorously evaluated the association between domain swapping and protein folding/unfolding. Here, we examined a kinetic model in which domain swapping occurred via the denatured state produced by the complete unfolding of proteins. The relationships between swapping kinetics and folding/unfolding thermodynamics were established, which were further adopted as criteria to show that the proposed mechanism dominates in three representative proteins: Cyanovirin-N (CV-N), the C-terminal domain of SARS-CoV main protease (Mpro-C), and a single mutant of oxidized thioredoxin (Trx_W28Aox).