Folding And Self-Assembly Of A Small Heterotetramer

dc.contributor.author	Yaşar , Fatih
dc.contributor.author	Sieradzan , Adam K.
dc.contributor.author	Hansmann , Ulrich H. E.
dc.date.accessioned	2019-12-13T06:31:01Z
dc.date.available	2019-12-13T06:31:01Z
dc.date.issued	2014
dc.identifier.issn	0021-9606
dc.identifier.uri	https://doi.org/10.1063/1.4868140
dc.identifier.uri	http://hdl.handle.net/11655/18343
dc.description.abstract	Designed miniproteins offer a possibility to study folding and association of protein complexes, both experimentally and in silico. Using replica exchange molecular dynamics and the coarse-grain UNRES force field, we have simulated the folding and self-assembly of the heterotetramer BBAThet1, comparing it with that of the homotetramer BBAT1 which has the same size and beta beta alpha-fold. For both proteins, association of the tetramer precedes and facilitates folding of the individual chains. (C) 2014 AIP Publishing LLC.
dc.language.iso	en
dc.publisher	Amer Inst Physics
dc.relation.isversionof	10.1063/1.4868140
dc.rights	info:eu-repo/semantics/openAccess
dc.subject	Chemistry
dc.subject	Physics
dc.title	Folding And Self-Assembly Of A Small Heterotetramer
dc.type	info:eu-repo/semantics/article
dc.type	info:eu-repo/semantics/publishedVersion
dc.relation.journal	Journal Of Chemical Physics
dc.contributor.department	Fizik Mühendisliği
dc.identifier.volume	140
dc.identifier.issue	10
dc.description.index	WoS