The dynamics of multimer formation of the amphiphilic hydrophobin protein HFBII

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dc.contributor Aalto-yliopisto fi
dc.contributor Aalto University en
dc.contributor.author Grunér, M.S.
dc.contributor.author Paananen, A.
dc.contributor.author Szilvay, Géza R.
dc.contributor.author Linder, M. B.
dc.date.accessioned 2017-06-20T11:14:42Z
dc.date.available 2017-06-20T11:14:42Z
dc.date.issued 2017-07-01
dc.identifier.citation Grunér , M S , Paananen , A , Szilvay , G R & Linder , M B 2017 , ' The dynamics of multimer formation of the amphiphilic hydrophobin protein HFBII ' COLLOIDS AND SURFACES B: BIOINTERFACES , vol 155 , pp. 111-117 . DOI: 10.1016/j.colsurfb.2017.03.057 en
dc.identifier.issn 0927-7765
dc.identifier.issn 1873-4367
dc.identifier.other PURE UUID: 1e9f95c4-3f14-4dd9-b4b2-5d291881d96d
dc.identifier.other PURE ITEMURL: https://research.aalto.fi/en/publications/the-dynamics-of-multimer-formation-of-the-amphiphilic-hydrophobin-protein-hfbii(1e9f95c4-3f14-4dd9-b4b2-5d291881d96d).html
dc.identifier.other PURE LINK: http://www.scopus.com/inward/record.url?scp=85017434474&partnerID=8YFLogxK
dc.identifier.other PURE FILEURL: https://research.aalto.fi/files/13409017/Dynamics_of_multimer_formation_of_the_amphiphilic_Linder_2017.pdf
dc.identifier.uri https://aaltodoc.aalto.fi/handle/123456789/26939
dc.description This work wassupported by the Academy of Finland through its Centres of Excel-lence Programme (2014–2019) and under Projects No. 259034 and264493.
dc.description.abstract Hydrophobins are surface-active proteins produced by filamentous fungi. They have amphiphilic structures and form multimers in aqueous solution to shield their hydrophobic regions. The proteins rearrange at interfaces and self-assemble into films that can show a very high degree of structural order. Little is known on dynamics of multimer interactions in solution and how this is affected by other components. In this work we examine the multimer dynamics by stopped-flow fluorescence measurements and Förster Resonance Energy Transfer (FRET) using the class II hydrophobin HFBII. The half-life of exchange in the multimer state was 0.9 s at 22 °C with an activation energy of 92 kJ/mol. The multimer exchange process of HFBII was shown to be significantly affected by the closely related HFBI hydrophobin, lowering both activation energy and half-life for exchange. Lower molecular weight surfactants interacted in very selective ways, but other surface active proteins did not influence the rates of exchange. The results indicate that the multimer formation is driven by specific molecular interactions that distinguish different hydrophobins from each other. en
dc.format.extent 7
dc.format.extent 111-117
dc.format.mimetype application/pdf
dc.language.iso en en
dc.relation.ispartofseries COLLOIDS AND SURFACES B: BIOINTERFACES en
dc.relation.ispartofseries Volume 155 en
dc.rights openAccess en
dc.subject.other Biotechnology en
dc.subject.other Surfaces and Interfaces en
dc.subject.other Physical and Theoretical Chemistry en
dc.subject.other Colloid and Surface Chemistry en
dc.subject.other 1182 Biochemistry, cell and molecular biology en
dc.title The dynamics of multimer formation of the amphiphilic hydrophobin protein HFBII en
dc.type A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä fi
dc.description.version Peer reviewed en
dc.contributor.department VTT Technical Research Centre of Finland
dc.contributor.department Department of Bioproducts and Biosystems
dc.subject.keyword Fluorescence
dc.subject.keyword FRET
dc.subject.keyword Förster Resonance Energy Transfer
dc.subject.keyword HFBI
dc.subject.keyword HFBII
dc.subject.keyword Hydophobin
dc.subject.keyword Stopped-flow
dc.subject.keyword Surfactant
dc.subject.keyword Biotechnology
dc.subject.keyword Surfaces and Interfaces
dc.subject.keyword Physical and Theoretical Chemistry
dc.subject.keyword Colloid and Surface Chemistry
dc.subject.keyword 1182 Biochemistry, cell and molecular biology
dc.identifier.urn URN:NBN:fi:aalto-201706205663
dc.identifier.doi 10.1016/j.colsurfb.2017.03.057
dc.type.version publishedVersion


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