{"id":3033,"date":"2020-02-14T08:26:07","date_gmt":"2020-02-14T07:26:07","guid":{"rendered":"https:\/\/blogs.urz.uni-halle.de\/irtgpolymers\/?p=3033"},"modified":"2020-02-26T19:36:25","modified_gmt":"2020-02-26T18:36:25","slug":"doctoral-students-seminar-february-25-2020","status":"publish","type":"post","link":"https:\/\/blogs.urz.uni-halle.de\/irtgpolymers\/2020\/02\/doctoral-students-seminar-february-25-2020\/","title":{"rendered":"Doctoral students seminar (February 25, 2020)"},"content":{"rendered":"\n<p><strong>Investigating chaperone activity and gelation of human aB eye lens crystallin protein using solid state NMR<\/strong><b><br><\/b>by Maria Camilles<\/p>\n\n\n\n<p><strong>Halbleitende Blockcopolymere und Modellsysteme: Der Einfluss von molekularem Aufbau und molekularer Dynamik auf die Strukturbildung<\/strong> (<strong>Rehearsal<\/strong>) by Matthias Fischer<\/p>\n\n\n\n<p>Location: Halle University, von-Danckelmann-Platz 3, SR 1.03<br>Time: 3.20pm-5.00pm<\/p>\n\n\n\n<!--more-->\n\n\n\n<p class=\"has-medium-font-size\"><strong>Abstracts<\/strong><\/p>\n\n\n\n<p><strong>Investigating chaperone activity and gelation of human aB eye lens crystallin protein using solid state NMR<\/strong><\/p>\n\n\n\n<p>Maria Camilles<\/p>\n\n\n\n<p>Crystallins are the major vision-related (i.e. refractive) proteins found in the eye lens. The mammalian lens consists of three classes of structural proteins, i.e a-, b- and g-crystallins. The former also acts as chaperone [1]. Commonly, proteins are subject to a continuous degradation and replacement process, but the eye lens proteins have to remain stable and soluble for a lifetime [2]. Heat shock or other stressors can cause aggregation and lead to cataract; thus, the major function of the chaperone is to prevent aggregation. Here we investigate aB-crystallin proteins which is highly expressed in both eye lens as well as muscle tissues and also widely known for its chaperoning ability. We use solid state MAS NMR (SS NMR) [3] to probe the changes that occur at a specific site when a target protein (gB-crystallin) binds to it and study the effect of protein concentrations on the protection ability of aB-crystallin proteins.<\/p>\n\n\n\n<p>In our previous work [4] we found out that a- crystallin upon aggregation forms a gel as opposed to gB crystallin which forms a solid precipitate. &nbsp;The studies based on a-crystallin gels are limited, so the mechanism of aggregation and gelation of these proteins are unclear. We would therefore also investigate the gelation of a-crystallin protein using SS NMR and the changes in the crystallin backbone are to be probed, which can clarify whether the a-crystallin loses it native structure or remains unaffected when it transforms into a gel. Then the aim here is to correlate rheology, Electron Microscopy and MAS NMR to investigate the effect of protein concentration and ionic strengths on the gelation of haB crystallin. This should give some insights into the mechanism and dynamic properties of the a-crystallin protein gel.<\/p>\n\n\n\n<p>References:<\/p>\n\n\n\n<p>[1] Bloemendal, H.<em> et al.<\/em> Ageing and vision: structure, stability and function of lens crystallins, <em>Biophys. Mol.Biol.<\/em> 2004, 86:407\u2013485.<\/p>\n\n\n\n<p>[2] Delaye, M. Tardieu, A., Short-range order of crystallin proteins accounts for eye lens transparency.<em>Nature<\/em>. 1983, 302:415\u2013417.<\/p>\n\n\n\n<p>[3] Mainz, A. <em>et al., <\/em>The chaperone aB-crystallin uses different interfaces to capture an amorphous and an amyloid client, <em>Struct. Mol. Biol., <\/em>2015, 22:898-908.<\/p>\n\n\n\n<p>[4] Camilles <em>et al., <\/em>Quantitative NMR study of heat-induced aggregation of eye-lems crystallin proteins under crowding conditions<em>, BBA Prot. Proteom., 2018, <\/em>1866: 1055-1061.<\/p>\n\n\n<p><\/p>\n<p><strong>Halbleitende Blockcopolymere und Modellsysteme: Der Einfluss von molekularem Aufbau und molekularer Dynamik auf die Strukturbildung<\/strong><\/p>\n<p>Matthias Fischer<\/p>\n<p>Die Versorgung der Weltbev\u00f6lkerung mit regenerativen Energien stellt eine der gr\u00f6\u00dften Herausforderungen des 21. Jahrhunderts dar. Organische Solarzellen k\u00f6nnen dank niedriger Herstellungs- und Verarbeitungskosten, ihrer mechanische Flexibilit\u00e4t und eines geringen Gewichts dazu einen entscheidenden Beitrag leisten. F\u00fcr eine hohe Effizienz und dementsprechend eine gute Ladungstr\u00e4gerseparation ist jedoch eine nanostrukturierte Morphologie mit Grenzfl\u00e4chen zwischen einem Lochleiter- (Donor) und einem Elektronenleitermaterial (Akzeptor) auf der Gr\u00f6\u00dfenordnung von wenigen 10 nm notwendig. Dieser Vortrag widmet sich dem Einfluss der chemischen Struktur und der molekularen Dynamik auf die Mikrophasenseparation der Blockcopolymere und die Kristallisation der Homopolymere. Dazu werden die Ergebnisse der Charakterisierung zweier Materialsysteme von Donor-Akzeptor-Blockcopolymeren und der zugrundeliegenden Homopolymere vorgestellt: genutzt werden ein Poly(3-hexylthiophen) (<strong>P3HT<\/strong>)-haltiger Donor und ein [6,6]-Phenyl-C<sub>61<\/sub>-Butters\u00e4uremethylester (<strong>PCBM<\/strong>)- bzw. Perylenbisimid (<strong>PBI<\/strong>)-haltiger Akzeptor. Als zentrale Methoden der Strukturaufkl\u00e4rung wurden R\u00f6ntgenstreuung, dynamische Differenzkalorimetrie sowie verschiedene Mikroskopietechniken verwendet. Die Glas\u00fcbergangstemperatur wird als entscheidender Designparameter f\u00fcr die Ausbildung einer Mikrophasenseparation der Blockcopolymere, sowie einer fl\u00fcssigkristallinen Ordnung der Akzeptorpolymere und die Ladungstr\u00e4germobilit\u00e4t identifiziert. Des Weiteren zeigen die Ergebnisse die Bedeutung der Aggregation und der \u03c0-\u03c0-Orientierung f\u00fcr den Ladungstransport in halbleitenden Polymeren.<\/p>","protected":false},"excerpt":{"rendered":"<p>Investigating chaperone activity and gelation of human aB eye lens crystallin protein using solid state NMRby Maria Camilles &hellip; <a href=\"https:\/\/blogs.urz.uni-halle.de\/irtgpolymers\/2020\/02\/doctoral-students-seminar-february-25-2020\/\" class=\"more-link\">Continue reading<span class=\"screen-reader-text\"> &#8220;Doctoral students seminar (February 25, 2020)&#8221;<\/span><\/a><\/p>\n","protected":false},"author":4439,"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\/3033"}],"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\/4439"}],"replies":[{"embeddable":true,"href":"https:\/\/blogs.urz.uni-halle.de\/irtgpolymers\/wp-json\/wp\/v2\/comments?post=3033"}],"version-history":[{"count":9,"href":"https:\/\/blogs.urz.uni-halle.de\/irtgpolymers\/wp-json\/wp\/v2\/posts\/3033\/revisions"}],"predecessor-version":[{"id":3205,"href":"https:\/\/blogs.urz.uni-halle.de\/irtgpolymers\/wp-json\/wp\/v2\/posts\/3033\/revisions\/3205"}],"wp:attachment":[{"href":"https:\/\/blogs.urz.uni-halle.de\/irtgpolymers\/wp-json\/wp\/v2\/media?parent=3033"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/blogs.urz.uni-halle.de\/irtgpolymers\/wp-json\/wp\/v2\/categories?post=3033"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/blogs.urz.uni-halle.de\/irtgpolymers\/wp-json\/wp\/v2\/tags?post=3033"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}