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<p class="MsoTitle" style="margin:0cm;margin-bottom:.0001pt"><span lang="EN-US" style="font-size:14.0pt;font-family:"Verdana","sans-serif";color:black;font-weight:normal">VABILO NA PREGLOV KOLOKVIJ / INVITATION TO THE PREGL COLLOQUIUM<o:p></o:p></span></p>
<p class="MsoNormal"><b><span lang="EN-US" style="font-size:12.0pt;font-family:"Verdana","sans-serif""><o:p> </o:p></span></b></p>
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<b><span lang="EN-US" style="font-size:18.0pt;font-family:"Verdana","sans-serif"">Prof. Vincent P. Conticello, Ph.D.</span></b><span lang="EN-GB" style="font-size:8.0pt;font-family:"Verdana","sans-serif""><o:p></o:p></span></p>
<p align="center" style="margin:0cm;margin-bottom:.0001pt;text-align:center"><span lang="EN-GB" style="font-size:12.0pt;font-family:"Verdana","sans-serif"">Department of Chemistry, Emory University, Atlanta, USA<o:p></o:p></span></p>
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<p class="MsoNormal" align="center" style="text-align:center;line-height:150%"><b><span lang="EN-US" style="font-size:14.0pt;line-height:150%;font-family:"Verdana","sans-serif"">Torek / Tuesday 12. 05. 2015, ob / at 13:00
<o:p></o:p></span></b></p>
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<b><span lang="EN-US" style="font-size:11.0pt;font-family:"Verdana","sans-serif"">Velika predavalnica Kemijskega inštituta / Lecture Hall at the National Institute of Chemistry; Hajdrihova 19, Ljubljana</span></b><b><span lang="EN-US" style="font-size:12.0pt;font-family:"Verdana","sans-serif"">
<o:p></o:p></span></b></h6>
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<p class="MsoNormal" align="center" style="text-align:center"><b><span lang="EN-GB" style="font-size:20.0pt;font-family:"Verdana","sans-serif";color:#660066">Designability of Peptide-Based Materials<o:p></o:p></span></b></p>
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<span lang="EN-US" style="font-size:9.0pt;font-family:"Verdana","sans-serif";color:#660066"><o:p> </o:p></span></p>
<p class="MsoNormal" align="center" style="text-align:center"><span lang="FR" style="font-size:11.0pt;font-family:"Arial","sans-serif"">Structurally defined materials on the nanometer length-scale have been historically the most challenging to rationally construct
and the most difficult to structurally analyze. Sequence-specific biomolecules, i.e., proteins and nucleic acids, have advantages as design elements for construction of these types of nano-scale materials in that correlations can be drawn between sequence
and higher order structure, potentially affording ordered assemblies in which functional properties can be controlled through the progression of structural hierarchy encoded at the molecular level. However, the predictable design of self-assembled structures
requires precise structural control of the interfaces between peptide subunits (protomers). In contrast to the robustness of protein tertiary structure, quaternary structure has been postulated to be labile with respect to mutagenesis of residues located at
the protein-protein interface. We have employed simple self-assembling peptide systems to interrogate the concept of designability of interfaces within the structural context of nanotubes and nanosheets (see below). These peptide systems provide a framework
for understanding how minor sequence changes in evolution can translate into very large changes in supramolecular structure, which provides significant evidence that the designability of protein interfaces is a critical consideration for control of supramolecular
structure in self-assembling systems.<o:p></o:p></span></p>
<p class="MsoNormal"><span lang="FR"><o:p> </o:p></span></p>
<p class="MsoNormal"><span lang="FR"><o:p> </o:p></span></p>
<p class="MsoNormal"><span lang="FR"><o:p> </o:p></span></p>
<p class="MsoNormal" align="center" style="text-align:center;line-height:150%"><b><span lang="EN-US" style="font-size:14.0pt;line-height:150%;font-family:"Verdana","sans-serif"">Vljudno vabljeni! / Kindly invited!<o:p></o:p></span></b></p>
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