ArticleProtein science : a publication of the Protein Society2013
Evidences for the unfolding mechanism of three-dimensional domain swapping.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Human FoxP Transcription Factors as Tractable Models of the Evolution and Functional Outcomes of Three-Dimensional Domain Swapping.International journal of molecular sciences · 2021Review
- The protonation state of an evolutionarily conserved histidine modulates domainswapping stability of FoxP1.Scientific reports · 2019Article
- Hydrogen-deuterium exchange mass spectrometry reveals folding and allostery in protein-protein interactions.Methods (San Diego, Calif.) · 2018Review
- Exploring the Roles of Proline in Three-Dimensional Domain Swapping from Structure Analysis and Molecular Dynamics Simulations.The protein journal · 2018Article
- Understanding protein domain-swapping using structure-based models of protein folding.Progress in biophysics and molecular biology · 2017Review
- Three-Dimensional Domain Swapping Changes the Folding Mechanism of the Forkhead Domain of FoxP1.Biophysical journal · 2016Article
- Mechanism of 3D domain swapping in bovine seminal ribonuclease.The FEBS journal · 2014Article
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2 authors.
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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 (M(pro)-C), and a single mutant of oxidized thioredoxin (Trx_W28A(ox)).
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