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Stability of structurally entangled protein dimers
Author(s) -
Zhao Yani,
Cieplak Marek
Publication year - 2018
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.25526
Subject(s) - quantum entanglement , folding (dsp implementation) , chemical stability , chemistry , physics , chemical physics , biophysics , quantum mechanics , thermodynamics , biology , quantum , electrical engineering , engineering
We studied stretching, folding and thermodynamic properties of structurally entangled protein dimers. The tests for entanglement involve four‐terminal pulling. We study the dynamics of such pulling and contrast it with the standard two‐terminal one. The two‐chain entanglement is qualitatively characterized by its entangled core, which is defined as the minimal structure that is entangled. The existence of the entangled cores is found to be affecting both the mechanical and folding properties of the proteins. We also show that the folding pathways of the entangled proteins are not universal but the bottleneck is always the formation of the entangled conformation. We demonstrate that entanglement enhances thermodynamic stability.