Abstract:
:We carry out systematic Monte Carlo simulations of Gō lattice proteins to investigate and compare the folding processes of two model proteins whose native structures differ from each other due to the presence of a trefoil knot located near the terminus of one of the protein chains. We show that the folding time of the knotted fold is larger than that of the unknotted protein and that this difference in folding time is particularly striking in the temperature region below the optimal folding temperature. Both proteins display similar folding transition temperatures, which is indicative of similar thermal stabilities. By using the folding probability reaction coordinate as an estimator of folding progression we have found out that the formation of the knot is mainly a late folding event in our shallow knot system.
journal_name
Phys Bioljournal_title
Physical biologyauthors
Faísca PF,Travasso RD,Charters T,Nunes A,Cieplak Mdoi
10.1088/1478-3975/7/1/016009subject
Has Abstractpub_date
2010-02-03 00:00:00pages
16009issue
1eissn
1478-3967issn
1478-3975pii
S1478-3975(10)31787-0journal_volume
7pub_type
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