Publication:
Assembly of huntingtin headpiece into α-helical bundles

dc.contributor.departmentDepartment of Mechanical Engineering
dc.contributor.departmentDepartment of Chemical and Biological Engineering
dc.contributor.departmentGraduate School of Sciences and Engineering
dc.contributor.kuauthorÖzgür, Beytullah
dc.contributor.kuauthorSayar, Mehmet
dc.contributor.schoolcollegeinstituteCollege of Engineering
dc.contributor.schoolcollegeinstituteCollege of Sciences
dc.contributor.schoolcollegeinstituteGRADUATE SCHOOL OF SCIENCES AND ENGINEERING
dc.date.accessioned2024-11-09T13:47:28Z
dc.date.issued2017
dc.description.abstractProtein aggregation is a hallmark of neurodegenerative disorders. In this group of brain-related disorders, a disease-specific “host” protein or fragment misfolds and adopts a metastatic, aggregate-prone conformation. Often, this misfolded conformation is structurally and thermodynamically different from its native state. Intermolecular contacts, which arise in this non-native state, promote aggregation. In this regard, understanding the molecular principles and mechanisms that lead to the formation of such a non-native state and further promote the formation of the critical nucleus for fiber growth is essential. In this study, the authors analyze the aggregation propensity of Huntingtin headpiece (httNT), which is known to facilitate the polyQ aggregation, in relation to the helix mediated aggregation mechanism proposed by the Wetzel group. The authors demonstrate that even though httNT displays a degenerate conformational spectrum on its own, interfaces of macroscopic or molecular origin can promote the α-helix conformation, eliminating all other alternatives in the conformational phase space. Our findings indicate that httNT molecules do not have a strong orientational preference for parallel or antiparallel orientation of the helices within the aggregate. However, a parallel packed bundle of helices would support the idea of increased polyglutamine concentration, to pave the way for cross-β structures.
dc.description.fulltextYES
dc.description.indexedbyWOS
dc.description.indexedbyScopus
dc.description.indexedbyPubMed
dc.description.issue2
dc.description.openaccessYES
dc.description.publisherscopeInternational
dc.description.sponsoredbyTubitakEuTÜBİTAK
dc.description.sponsorshipScientific and Technological Research Council of Turkey (TÜBİTAK)
dc.description.versionPublisher version
dc.description.volume12
dc.identifier.doi10.1116/1.4984009
dc.identifier.eissn1559-4106
dc.identifier.embargoNO
dc.identifier.filenameinventorynoIR01221
dc.identifier.issn1934-8630
dc.identifier.quartileQ2
dc.identifier.scopus2-s2.0-85019741046
dc.identifier.urihttps://hdl.handle.net/20.500.14288/3769
dc.identifier.wos402049200001
dc.keywordsHTT protein
dc.keywordsHuntingtin protein
dc.keywordsPeptides
dc.keywordsPolyglutamine
dc.language.isoeng
dc.publisherAmerican Institute of Physics (AIP) Publishing
dc.relation.grantnoProject No. 116Z512
dc.relation.ispartofApplied Physics Letters
dc.relation.urihttp://cdm21054.contentdm.oclc.org/cdm/ref/collection/IR/id/2572
dc.subjectMultidisciplinary chemistry
dc.titleAssembly of huntingtin headpiece into α-helical bundles
dc.typeJournal Article
dspace.entity.typePublication
local.contributor.kuauthorÖzgür, Beytullah
local.contributor.kuauthorSayar, Mehmet
local.publication.orgunit1GRADUATE SCHOOL OF SCIENCES AND ENGINEERING
local.publication.orgunit1College of Engineering
local.publication.orgunit1College of Sciences
local.publication.orgunit2Department of Mechanical Engineering
local.publication.orgunit2Department of Chemical and Biological Engineering
local.publication.orgunit2Graduate School of Sciences and Engineering
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