Publication:
Prediction of optimal folding routes of proteins that satisfy the principle of lowest entropy loss: dynamic contact maps and optimal control

dc.contributor.departmentDepartment of Computer Engineering
dc.contributor.departmentDepartment of Chemical and Biological Engineering
dc.contributor.kuauthorArkun, Yaman
dc.contributor.kuauthorErman, Burak
dc.contributor.kuprofileFaculty Member
dc.contributor.kuprofileFaculty Member
dc.contributor.otherDepartment of Computer Engineering
dc.contributor.otherDepartment of Chemical and Biological Engineering
dc.contributor.schoolcollegeinstituteCollege of Engineering
dc.contributor.yokid108526
dc.contributor.yokid179997
dc.date.accessioned2024-11-09T13:27:14Z
dc.date.issued2010
dc.description.abstractAn optimization model is introduced in which proteins try to evade high energy regions of the folding landscape, and prefer low entropy loss routes during folding. We make use of the framework of optimal control whose convenient solution provides practical and useful insight into the sequence of events during folding. We assume that the native state is available. As the protein folds, it makes different set of contacts at different folding steps. The dynamic contact map is constructed from these contacts. The topology of the dynamic contact map changes during the course of folding and this information is utilized in the dynamic optimization model. The solution is obtained using the optimal control theory. We show that the optimal solution can be cast into the form of a Gaussian Network that governs the optimal folding dynamics. Simulation results on three examples (CI2, Sso7d and Villin) show that folding starts by the formation of local clusters. Non-local clusters generally require the formation of several local clusters. Non-local clusters form cooperatively and not sequentially. We also observe that the optimal controller prefers "zipping" or small loop closure steps during folding. The folding routes predicted by the proposed method bear strong resemblance to the results in the literature.
dc.description.fulltextYES
dc.description.indexedbyWoS
dc.description.indexedbyScopus
dc.description.indexedbyPubMed
dc.description.issue10
dc.description.openaccessYES
dc.description.publisherscopeInternational
dc.description.sponsoredbyTubitakEuN/A
dc.description.sponsorshipN/A
dc.description.versionPublisher version
dc.description.volume5
dc.formatpdf
dc.identifier.doi10.1371/journal.pone.0013275
dc.identifier.eissn1932-6203
dc.identifier.embargoNO
dc.identifier.filenameinventorynoIR00826
dc.identifier.issn1932-6203
dc.identifier.linkhttps://doi.org/10.1371/journal.pone.0013275
dc.identifier.quartileQ2
dc.identifier.scopus2-s2.0-78149455443
dc.identifier.urihttps://hdl.handle.net/20.500.14288/3509
dc.identifier.wos282807300014
dc.keywordsChymotrypsin Inhibitor-2
dc.keywords2-State Proteins
dc.keywordsTransition-State
dc.keywordsPathways
dc.keywordsMechanism
dc.keywordsRates
dc.keywordsModel
dc.languageEnglish
dc.publisherPublic Library of Science
dc.relation.urihttp://cdm21054.contentdm.oclc.org/cdm/ref/collection/IR/id/831
dc.sourcePLOS One
dc.subjectMultidisciplinary sciences
dc.titlePrediction of optimal folding routes of proteins that satisfy the principle of lowest entropy loss: dynamic contact maps and optimal control
dc.typeJournal Article
dspace.entity.typePublication
local.contributor.authorid0000-0002-3740-379X
local.contributor.authorid0000-0002-2496-6059
local.contributor.kuauthorArkun, Yaman
local.contributor.kuauthorErman, Burak
relation.isOrgUnitOfPublication89352e43-bf09-4ef4-82f6-6f9d0174ebae
relation.isOrgUnitOfPublicationc747a256-6e0c-4969-b1bf-3b9f2f674289
relation.isOrgUnitOfPublication.latestForDiscovery89352e43-bf09-4ef4-82f6-6f9d0174ebae

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