<html><head></head><body style="word-wrap: break-word; -webkit-nbsp-mode: space; -webkit-line-break: after-white-space; color: rgb(0, 0, 0); font-size: 14px; font-family: Calibri, sans-serif; "><div><br></div><span id="OLK_SRC_BODY_SECTION"><div xmlns:v="urn:schemas-microsoft-com:vml" xmlns:o="urn:schemas-microsoft-com:office:office" xmlns:w="urn:schemas-microsoft-com:office:word" xmlns:m="http://schemas.microsoft.com/office/2004/12/omml" xmlns="http://www.w3.org/TR/REC-html40"><div lang="EN-US" link="blue" vlink="purple"><div class="WordSection1"><p class="MsoNormal"><o:p> </o:p></p><p class="MsoNormal" align="center" style="mso-margin-top-alt:auto;margin-bottom:6.0pt;text-align:center;line-height:18.0pt"><a name="_Toc434675189"><b><span style="font-size: 14pt; font-family: 'Times New Roman', serif; color: black; ">PhD DEFENSE STUDENT: </span></b></a><span style="font-size: 14pt; font-family: 'Times New Roman', serif; color: black; ">Maria
Vorontsova Kaissaratos</span><span style="font-size: 14pt; font-family: 'Times New Roman', serif; color: black; "><o:p></o:p></span></p><p class="MsoNormal" align="center" style="mso-margin-top-alt:auto;margin-bottom:6.0pt;text-align:center;line-height:18.0pt"><b><span style="font-size: 14pt; font-family: 'Times New Roman', serif; color: black; ">DATE: </span></b><span style="font-size: 14pt; font-family: 'Times New Roman', serif; color: black; ">Friday,<b></b>April 22, 2016</span><span style="font-size: 14pt; font-family: 'Times New Roman', serif; color: black; "><o:p></o:p></span></p><p class="MsoNormal" align="center" style="mso-margin-top-alt:auto;margin-bottom:6.0pt;text-align:center;line-height:18.0pt"><b><span style="font-size: 14pt; font-family: 'Times New Roman', serif; color: black; ">TIME: </span></b><span style="font-size: 14pt; font-family: 'Times New Roman', serif; color: black; ">3:00 PM</span><span style="font-size: 14pt; font-family: 'Times New Roman', serif; color: black; "><o:p></o:p></span></p><p class="MsoNormal" align="center" style="mso-margin-top-alt:auto;margin-bottom:6.0pt;text-align:center;line-height:18.0pt"><b><span style="font-size: 14pt; font-family: 'Times New Roman', serif; color: black; ">PLACE: </span></b><span style="font-size: 14pt; font-family: 'Times New Roman', serif; color: black; ">Engineering Bldg. 2,
Room<b> </b>W205</span><span style="font-size: 14pt; font-family: 'Times New Roman', serif; color: black; "><o:p></o:p></span></p><p class="MsoNormal" align="center" style="mso-margin-top-alt:auto;margin-bottom:6.0pt;text-align:center;line-height:18.0pt"><b><span style="font-size: 14pt; font-family: 'Times New Roman', serif; color: black; ">DISSERTATION CHAIR: </span></b><span style="font-size: 14pt; font-family: 'Times New Roman', serif; color: black; ">Dr. Peter
Vekilov</span><span style="font-size: 14pt; font-family: 'Times New Roman', serif; color: black; "><o:p></o:p></span></p><div style="margin-bottom:10.0pt"><div class="MsoNormal" align="center" style="margin-bottom:0in;margin-bottom:.0001pt;text-align:center"><b><span style="font-size: 14pt; line-height: 115%; font-family: 'Times New Roman', serif; color: black; "><hr size="2" width="100%" align="center"></span></b></div></div><p class="MsoNormal" align="center" style="text-align:center"><b><span style="font-size: 14pt; line-height: 115%; font-family: 'Times New Roman', serif; color: black; ">TITLE:<o:p></o:p></span></b></p><p class="MsoNormal" align="center" style="margin-bottom:12.0pt;text-align:center;line-height:150%"><b><span style="font-size: 14pt; line-height: 150%; font-family: 'Times New Roman', serif; letter-spacing: 2pt; ">Physicochemical Aspects of the Two-Step Mechanism of Nucleation in Protein Solutions<o:p></o:p></span></b></p><p class="MsoNormal" style="text-align:justify;line-height:200%"><span style="font-size: 12pt; line-height: 200%; font-family: 'Times New Roman', serif; ">Protein-rich liquid clusters exist in solutions of numerous proteins. They play the role of nucleation precursors
of ordered solids of both folded proteins and partially misfolded chains. Examples include protein crystals, sickle-cell hemoglobin polymers, and amyloid fibrils. The clusters hold the key to the understanding and control of protein aggregation, and hence
insights of their physical properties is needed for development of successful crystallization recipes.<o:p></o:p></span></p><p class="MsoNormal" style="margin-bottom:0in;margin-bottom:.0001pt;text-align:justify;text-indent:.5in;line-height:200%"><span style="font-size: 12pt; line-height: 200%; font-family: 'Times New Roman', serif; ">We prove that protein clusters are not the nuclei of the dense liquid but rather represent a new phase which exists in homogeneous field of the protein phase diagram. With
nuclear magnetic resonance method we find the regions of protein molecules flexibility, potentially participating in cluster formation. We prove that water structuring interactions and partial protein unfolding contribute to clustering. We show that common
organic additives used in crystallization increase cluster volume fraction and surface area. The tests of insulin protein solutions explain why the two-step mechanism of nucleation is selected.
<o:p></o:p></span></p><p class="MsoNormal" style="margin-bottom:0in;margin-bottom:.0001pt;text-align:justify;text-indent:.5in;line-height:200%"><span style="font-size: 12pt; line-height: 200%; font-family: 'Times New Roman', serif; ">We develop a new spatial cross-correlation tracking method suitable for large (> $B&K(B/2) clusters. Monitoring of shape variations of intensity patterns of a single cluster indicates
that protein clusters are liquid. We employ depolarized oblique illumination microscopy to study the nucleation process and we show that crystals of lysozyme and glucose isomerase proteins indeed nucleate within protein-rich liquid clusters. These are the
first experiments of a direct observation of a two-step mechanism of nucleation in protein solutions.<b><o:p></o:p></b></span></p></div></div></div></span><style><!--
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