Bilayer thickness determines the alignment of model polyproline helices in lipid membranes

dc.contributor.authorKubyshkin, Vladimir
dc.contributor.authorGrage, Stephan L.
dc.contributor.authorUlrich, Anne S.
dc.contributor.authorBudisa, Nediljko
dc.date.accessioned2020-06-15T06:14:03Z
dc.date.available2020-06-15T06:14:03Z
dc.date.issued2019-09-18
dc.description.abstractOur understanding of protein folds relies fundamentally on the set of secondary structures found in the proteomes. Yet, there also exist intriguing structures and motifs that are underrepresented in natural biopolymeric systems. One example is the polyproline II helix, which is usually considered to have a polar character and therefore does not form membrane spanning sections of membrane proteins. In our work, we have introduced specially designed polyproline II helices into the hydrophobic membrane milieu and used 19F NMR to monitor the helix alignment in oriented lipid bilayers. Our results show that these artificial hydrophobic peptides can adopt several different alignment states. If the helix is shorter than the thickness of the hydrophobic core of the membrane, it is submerged into the bilayer with its long axis parallel to the membrane plane. The polyproline helix adopts a transmembrane alignment when its length exceeds the bilayer thickness. If the peptide length roughly matches the lipid thickness, a coexistence of both states is observed. We thus show that the lipid thickness plays a determining role in the occurrence of a transmembrane polyproline II helix. We also found that the adaptation of polyproline II helices to hydrophobic mismatch is in some notable aspects different from α-helices. Finally, our results prove that the polyproline II helix is a competent structure for the construction of transmembrane peptide segments, despite the fact that no such motif has ever been reported in natural systems.en
dc.description.sponsorshipDFG, 207100805, FOR 1805: Einfluss der Ribosomendynamik auf Regulation der Geschwindigkeit und Genauigkeit der Translationen
dc.description.sponsorshipTU Berlin, Open-Access-Mittel - 2019en
dc.identifier.eissn1463-9084
dc.identifier.issn1463-9076
dc.identifier.urihttps://depositonce.tu-berlin.de/handle/11303/11336
dc.identifier.urihttp://dx.doi.org/10.14279/depositonce-10223
dc.language.isoenen
dc.rights.urihttps://creativecommons.org/licenses/by/3.0/en
dc.subject.ddc540 Chemie und zugeordnete Wissenschaftende
dc.subject.otherpolyproline helixen
dc.subject.otherbilayer thicknessen
dc.subject.otherlipid thicknessen
dc.subject.othernatural biopolymeric systemsen
dc.subject.otheralignment statesen
dc.titleBilayer thickness determines the alignment of model polyproline helices in lipid membranesen
dc.typeArticleen
dc.type.versionpublishedVersionen
dcterms.bibliographicCitation.doi10.1039/C9CP02996Fen
dcterms.bibliographicCitation.journaltitlePhysical Chemistry Chemical Physicsen
dcterms.bibliographicCitation.originalpublishernameRSC Publishingen
dcterms.bibliographicCitation.originalpublisherplaceCambridgeen
dcterms.bibliographicCitation.pageend22408en
dcterms.bibliographicCitation.pagestart22396en
dcterms.bibliographicCitation.volume21en
tub.accessrights.dnbfreeen
tub.affiliationFak. 2 Mathematik und Naturwissenschaften>Inst. Chemie>FG Biokatalysede
tub.affiliation.facultyFak. 2 Mathematik und Naturwissenschaftende
tub.affiliation.groupFG Biokatalysede
tub.affiliation.instituteInst. Chemiede
tub.publisher.universityorinstitutionTechnische Universität Berlinen
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