Martin Kordts on “Triangulating protein-liposome interactions with EPR spectroscopy”
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Location:\nMartin-Luther-Universit\u00e4t Halle-Wittenberg \nTheodor-Lieser-Stra\u00dfe 9,\u00a0SR 1.03<\/b>\u00a0<\/b>(the lecture hall building)<\/span>,
06120 Halle (Saale) \nTime: 3.20pm - 5.00pm<\/strong> \n\nLink to OpenStreetMap<\/a><\/pre>\nAbstracts<\/h3>\n\n\n\nTriangulating protein-liposome interactions with EPR spectroscopy<\/h5>\n
by Martin Kordts<\/p>\n
\n\n\nHydrophobins are highly surface active fungal proteins of low molecular mass (<20 kDa) that self-assemble at interfaces. Based on hydropathy plots, solubility and superstructure morphology they are divided into two classes: class I (flexible monomers that fibrillate) and class II (compact momomers forming highly ordered membranes)[1, 2]. One of their presumed roles during the fungal life cycle is their involvement in the infection of a host organism by masking pathogenic compounds in order to suppress immune response and facilitate contact between the fungus and the host. [3, 4] We studied the interaction of class I hydrophobin SC3 from S. commune<\/i> and class II hydrophobin HFB2 from T. reesei <\/i>with simple liposomes as a model for cell membranes applying continuous wave electron paramagnetic resonance (cwEPR) spectroscopy. A \u201ctriangulation approach\u201c was taken by introducing the necessary paramagnetic species as either (1<\/b>) a guest molecule (16-doxyl stearic acid; 16-DSA<\/b>) within the liposome, (2<\/b>) part of the lipid bilayer, or (3<\/b>) covalently attached to HFB2.<\/p>\n
Choosing the gaugeable component of a complex system in such a way allows for a detailed view of the underlying mechanics on a molecular level at low cost and with high precision.<\/p>\n
References<\/b><\/p>\n
[1] Linder, M.B., Hydrophobins: Proteins that self assemble at interfaces.<\/i> Current Opinion in Colloid & Interface Science, 2009. 14<\/b>(5): p. 356-363.<\/p>\n
[2] Bayry, J., et al., Hydrophobins–unique fungal proteins.<\/i> PLoS pathogens, 2012. 8<\/b>(5): p. e1002700-e1002700.<\/p>\n
[3] Aimanianda, V., et al., Surface hydrophobin prevents immune recognition of airborne fungal spores.<\/i> Nature, 2009. 460<\/b>(7259): p. 1117-21.<\/p>\n
[4] W\u00f6sten, H.A.B., Hydrophobins: Multipurpose Proteins.<\/i> Annual Review of Microbiology, 2001. 55<\/b>(1): p. 625-646.<\/p>\n<\/div>\n<\/div>\n<\/div>\n<\/div>\n<\/div>\n<\/div>\n","protected":false},"excerpt":{"rendered":"","protected":false},"author":4475,"featured_media":0,"comment_status":"open","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"ngg_post_thumbnail":0},"categories":[99,90],"tags":[],"_links":{"self":[{"href":"https:\/\/blogs.urz.uni-halle.de\/irtgpolymers\/wp-json\/wp\/v2\/posts\/2888"}],"collection":[{"href":"https:\/\/blogs.urz.uni-halle.de\/irtgpolymers\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/blogs.urz.uni-halle.de\/irtgpolymers\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/blogs.urz.uni-halle.de\/irtgpolymers\/wp-json\/wp\/v2\/users\/4475"}],"replies":[{"embeddable":true,"href":"https:\/\/blogs.urz.uni-halle.de\/irtgpolymers\/wp-json\/wp\/v2\/comments?post=2888"}],"version-history":[{"count":5,"href":"https:\/\/blogs.urz.uni-halle.de\/irtgpolymers\/wp-json\/wp\/v2\/posts\/2888\/revisions"}],"predecessor-version":[{"id":2950,"href":"https:\/\/blogs.urz.uni-halle.de\/irtgpolymers\/wp-json\/wp\/v2\/posts\/2888\/revisions\/2950"}],"wp:attachment":[{"href":"https:\/\/blogs.urz.uni-halle.de\/irtgpolymers\/wp-json\/wp\/v2\/media?parent=2888"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/blogs.urz.uni-halle.de\/irtgpolymers\/wp-json\/wp\/v2\/categories?post=2888"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/blogs.urz.uni-halle.de\/irtgpolymers\/wp-json\/wp\/v2\/tags?post=2888"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}