ÿþ<!DOCTYPE html PUBLIC "-//W3C//DTD XHTML 1.0 Strict//EN" "http://www.w3.org/TR/xhtml1/DTD/xhtml1-strict.dtd"> <html> <head> <title>Liliya Vugmeyster's professional webpage</title> <link rel="stylesheet" type="text/css" href="index.css" /> </head> <body> <div id="letterhead"> <div id="name"> Liliya Vugmeyster </div> <div id="address"> Assistant Professor, Department of Chemistry<br /> Faculty Fellow, Environmental and Natural Resources Institute<br /> University of Alaska Anchorage </div> <div id="contact"> aflv@uaa.alaska.edu <br /> phone (907)-786-4709 </div> </div> <div id="navigation"> <ul> <li><a href="#education">Education</a></li> <li><a href="#work">Appointments</a></li> <li><a href="#collaboration">Collaborators</a></li> <li><a href="#undergraduates">Students</a></li> <li><a href="#teaching">Teaching</a></li> <li><a href="#research">Research</a></li> <li><a href="#publications">Publications</a></li> <li><a href="#grants">Funding</a></li> </ul> </div> <div id="photo"> <img src="eaglelake.jpg" alt="on Eagle Lake" width="450" height="338" /> </div> <div id="cv"> <div id="education"> <h2>EDUCATION</h2> <p>Lehman College, City University of New York NY, Chemistry, B.S., 1996</p> <p>State University of New York at Stony Brook , Chemistry, Ph. D., 2001<br /> Title of thesis: <em>Studies in protein folding and dynamics using magnetic resonance spectroscopy.</em><br /> Thesis supervisors: Prof. Daniel P. Raleigh, SUNY at Stony Brook,<br /> Prof. Arthur G. Palmer, Columbia University. </p> </div> <div id="work"> <h2>Postdoctoral and other appointments</h2> <p>Visiting Scientist, Laboratory of Prof. James McKnight Boston University School of Medicine, Boston, MA, 2006</p> <p>Postdoctoral, Laboratory of Prof. Judith Herzfeld, Brandeis University, Waltham MA, 2005 </p> <p>Postdoctoral, Laboratory of Prof. Geoffrey Bodenhausen, Ecole Polytechnique Fédérale de Lausanne, Switzerland, 2002-2004 </p> <p>Visiting Scientist, Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge MA 2004-2005</p> </div> <div id="collaboration"> <h2>COLLABORATORS</h2> <p> <ul> <li>Gina L.Hoatson, Robert L. Vold, College of William and Mary</li> <li>Dmitry Ostrovsky, University of Alaska Anchorage</li> <li>Arthur G. Palmer, Ying Li, Columbia University</li> <li>James C. McKnight, Boston University School of Medicine</li> <li>Joseph Ford, Andrew Lipton, Sarah Burton, Pacific Northwest National Laboratory</li> <li>Serge Smirnov, Western Washington University</li> </ul> </p> </div> <div id="undergraduates"> <h2>RECENT UNDERGRADUATE STUDENTS</h2> <p>current students: Tien Do, Kirsten Penland, Michael Hammond.</p> <p>past students: Derek Clark, Philip Hayes, Mark Moses, Anastasia Khadjinova.</p> </div> <div id="teaching"> <h2>TEACHING</h2> <p><em>Classes taught:</em><br /> General Chemistry, Concepts in Chemistry, Survey of Chemistry, Survey of Chemistry Laboratory <br /> Physical Chemistry, Physical Chemistry Laboratory. </p> <p><em>Current teaching goals:</em> show students a variety of approaches for learning physical sciences, let them develop their own learning skills and strategies for understanding basic concepts and complex theories. Share with students a constant sense of curiosity and fascination about science.</p> </div> <div id="research"> <h2>RESEARCH INTERESTS</h2> <p><strong>Dynamics and folding of proteins using solution and solid-state nuclear magnetic resonance techniques and theoretical/computational approaches. </strong></p> <p>One of the proteins I look at is a classic model system of protein folding studies: chicken villin headpiece subdomain (HP35). It is a small protein consisting of 35 amino acids which span three helices. The ribbon diagram is shown in the figure below.</p> <img src="HP35.jpg" alt="HP35 ribbon diagram" width="183" height="197" /> <p>Three-dimensional molecular shapes of proteins have been long recognized to play an important role in their biological functions. Many structural studies have been performed that aim at finding exact structures of proteins. In the past decade it became clear that protein molecules  breathe and their structures fluctuate. It turned out that this breathing has important consequences for specific functions and characteristics of proteins.</p> <p>My studies investigate the dynamics of proteins on various time scales and at various conditions: in solution and solids phases, at temperatures from 4K to 300K by experimental and computational approaches. </p> <p>Nuclear Magnetic Resonance (NMR) techniques are particularly suitable for the investigation of protein dynamics, since they allow measurements at many sites on a protein molecule, thus providing us with the picture of what s going on in various parts of the protein. Further, these techniques can be sensitive to motions over a very broad range of time scales, from picoseconds (10<SUP>-9</SUP>sec) to seconds. I use NMR as a major experimental tool to probe protein dynamics. In addition, I use a number of theoretical and computation approaches for data analysis and interpretation.</p> <p><strong>Determination of Unfrozen Water Content and Mechanisms of its Survival in Soils of the Dry Valleys of Antarctica by Nuclear Magnetic Resonance </strong></p> <p>Subsurface ice and salt are very common in soils of the Dry Valleys, Antarctica. Evidence based on chemical analysis points to the existence of unfrozen water. Reasons for the considerable interest in the formation and stability of subsurface ice and water stem from their crucial role in the genesis of landscapes and formation and survival of life. Ice is critical to the development of polygonal patterned ground surfaces in Antarctic Dry Valleys that serve as an analogue to Martian surfaces where subsurface ice has recently been confirmed by the Phoenix Mars Lander. Antarctic soils serve as a testing ground to develop models for ice and water formation and their survival mechanisms. We will conduct a preliminary study of the content of the unfrozen water in frozen ground of the Dry Valleys, the dependence of the amount of water on salt concentration and composition, as well as factors contributing to the mechanisms of its formation and survival.</p> <img src="bruker.jpg" alt="Bruker 750MHz magnet in College of William and Mary" width="300" height="400" /> </div> <div id="publications"> <h2>LIST OF PUBLICATIONS</h2> <ol> <li> <span class="authors">Vugmeyster L, Do T, Ostrovsky D, Fu R, Hagedorn B,</span> <span class="journal"><em>submitted to Solid State NMR</em>(2012)</span> <span class="title">Characterization of Water Dynamics in Frozen Soils by Solid-State Deuteron NMR </span> </li> <li> <span class="authors">Vugmeyster L, Ostrovsky D, Hoatson GL, Vold RL, </span> <span class="journal"><em>submitted to Biophys. J. </em>(2012)</span> <span class="title">Glassy Dynamics of Methyl groups in Chicken Villin Headpiece Subdomain Protein Revealed by Deuteron NMR relaxation</span> </li> <li> <span class="authors">Vugmeyster L, Ostrovsky D, Khadjinova A, Ellden J, Hoatson GL, Vold RL, </span> <span class="journal">Biochemistry (2011), 50 (49), 110637-10646 </span> <span class="title">Slow motions in the hydrophobic core of chicken villin headpiece subdomain and their contributions to configurational entropy and heat capacity from solid-state deuteron NMR measurements </span> </li> <li> <span class="authors"> Vugmeyster L, Ostrovsky D, </span> <span class="journal"> J. Biomol. NMR, 50(2), 119-127 (2011) </span> <span class="title">Temperature Dependence of Fast Carbonyl Backbone Dynamics in Chicken Villin Headpiece Subdomain.</span>  </li> <li> <span class="authors"> Vugmeyster L, Ostrovsky D, Moses M, Ford JJ, Lipton AS, Hoatson GL, Vold RL, </span> <span class="journal"> J. Phys. Chem. 114 (48), 15799 15807 (2010) </span> <span class="title">Comparative Dynamics of Leucine Methyl Groups in FMOC-Leucine and in a Protein Hydrophobic Core Probed by Solid-State Deuteron NMR over 7-324K Temperature Range.</span>  </li> <li> <span class="authors"> Vugmeyster L, Ostrovsky D, Li Y, </span> <span class="journal"> J. Biomol. NMR 47 (2), 155-162 (2010) </span> <span class="title">Comparison of fast backbone dynamics at amide nitrogen and carbonyl sites In dematin headpiece C-terminal domain and Its S74E mutant.</span>  </li> <li> <span class="authors"> Vugmeyster L, Ostrovsky D, Ford JJ, Lipton AS, </span> <span class="journal"> J. Am. Chem. Soc. 132 (12), 4038 4039 (2010) </span> <span class="title">Freezing of dynamics of a methyl group in a protein hydrophobic core at cryogenic temperatures by deuteron NMR spectroscopy.</span>  </li> <li> <span class="authors"> Vugmeyster L, Ostrovsky D, Ford JJ, Burton SD, Lipton AS, Hoatson GL, Vold RL, </span> <span class="journal"> J. Am. Chem. Soc. 131 (38), 13651 13658 (2009) </span> <span class="title"> Probing the dynamics of a protein hydrophobic core by deuteron solid-state nuclear magnetic resonance spectroscopy.</span>  </li> <li> <span class="authors"> Vold RL, Hoatson GL, Vugmeyster L, Ostrovsky D, DeCasto PJ, </span> <span class="journal"> Phys. Chem. Chem. Phys. 11, 7008-7012 (2009) </span> <span class="title">Solid State Deuteron Relaxation Time Anisotropy Measured With Multiple Echo Acquisition.</span>  </li> <li> <span class="authors"> Vugmeyster L </span> <span class="journal"> Magn. Reson. Chem. 47, 746-751 (2009) </span> <span class="title">Slow Backbone Dynamics of Chicken Villin Headpiece Subdomain Probed by NMR C&prime;-N Cross-Correlated Relaxation.</span>  </li> <li> <span class="authors">Vugmeyster L, McKnight CJ, </span><span class="journal"> J Biomol NMR 43, 39-50 (2009) </span><span class="title">Phosphorylation-induced changes in backbone dynamics of dematin headpiece C-terminal subdomain.</span> </li> <li> <span class="authors">Vugmeyster L, McKnight CJ, </span><span class="journal"> Biophys J 95, 5941-5960 (2008) </span><span class="title">Slow Motions in Chicken Villin Headpiece Subdomain Probed by Cross-correlated NMR Relaxation of Amide NH Bonds in Successive Residues.</span> </li> <li> <span class="authors">Vugmeyster L, Bodenhausen G, </span><span class="journal">Appl Magn Reson 28, 147-163 (2005) </span><span class="title">Temperature dependent protein backbone dynamics from auto- and cross-correlated NMR relaxation rates.</span> </li> <li> <span class="authors">Vugmeyster L, Perazzolo C, Wist J, Frueh D, Bodenhausen G, </span><span class="journal">J Biomol NMR 28, (2), 173-177 (2004) </span><span class="title">Evidence of slow motions by cross-correlated chemical shift modulation in deuterated and protonated proteins.</span> </li> <li> <span class="authors">Vugmeyster L, Pelupessy P, Vugmeister BE, Abergel D, Bodenhausen G, </span><span class="journal">Comptes Rendus de l'Académie des Sciences (section de Physique) 5 (3), 377-386 (2004) </span><span class="title">Cross-correlated relaxation in NMR of macromolecules in the presence of fast and slow dynamics.</span> </li> <li> <span class="authors">Wang M, Tang Y, Sato S, Vugmeyster L, McKnight CJ, Raleigh DP, </span><span class="journal"> J Am Chem Soc 125 (20), 6032-6033 (2003) </span><span class="title">Dynamic NMR lineshape analysis demonstrates that the Villin Headpiece Domain folds on the microsecond time scale.</span> </li> <li> <span class="authors">Vugmeyster L, Raleigh DP, Palmer AG, Vugmeister BE, </span><span class="journal">J Am Chem Soc 125 (27), 8400-8404 (2003) </span><span class="title">Beyond the decoupling approximation in the model free approach for the interpretation of NMR relaxation of macromolecules in solution.</span> </li> <li> <span class="authors">Vugmeyster L, Trott O, McKnight CJ, Raleigh DP, Palmer AG, </span><span class="journal">J Mol Biol, 320 (4), 841-854 (2002) </span><span class="title">Temperature-dependent dynamics of the villin headpiece helical subdomain, an unusually small thermostable protein.</span> </li> <li> <span class="authors">Vugmeyster L, Kroenke CD, Picart F, Palmer AG, Raleigh DP, </span><span class="journal">J Am Chem Soc , 122 (22), 5387-5388 (2000) </span><span class="title"> N15 R1rho measurements allow the determination of ultrafast protein folding rates.</span> </li> <li> <span class="authors">Vugmeyster L, Kuhlman B, Raleigh DP, </span><span class="journal">Protein Science, 7 (9), 1994-1997 (1998)</span><span class="title"> Amide proton exchange measurements as a probe of the stability and dynamics of the N-terminal domain of the ribosomal protein L9: Comparison with the intact protein.</span> </li> </ol> </div> <div id="grants"> <h2>RESEARCH SUPPORT</h2> <ol><h3>Ongoing Research Support</h3> <li>NSF-RUI:  Probing the Free Energy Landscape of Hydrophobic Cores by Solid-State NMR. 9/1/2011-8/31/2014 $201,000 Role: PI. </li> <li>Research Corporation Cottrell College Award $39,000  Dynamics of Protein Hydrophobic Cores by Deuteron Solid-State NMR Spectroscopy 01/2010-12/2011. Role: PI. </li> <li>INBRE seed grant  Dynamics of Actin-binding Chicken Villin Headpiece Domain: The role of a buried salt bridge UAA 3/2012-2/2013 Role: PI.</li> <li>Alaska Space Grant Program  Follow the Water : Determination Of Unfrozen Water Content and Mechanisms Of Its Survival In Soils Of the Dry Valleys Of Antarctica By Nuclear Magnetic Resonance $21,194; 6/2011-5/2012 Role PI.</li> <li>Instrumentation time award at Pacific Northwest National Laboratory, 10/2011-10/2012. </li> <li>National High Field Magnetic Laboratory at Tallahassee, FL instrumentation time award, 6/2011  6/2012. </li> </ol> <ol><h3>Completed Research Support</h3> <li>NSF-ROA through the <em>supplement to the grant of Prof. Robert L. Vold</em>, College of William and Mary, CHE-0939970-S00012408,  Quantitative Studies of Molecular Dynamics in Solids by Nuclear Magnetic Resonance of Quadrupolar Nuclei 06/09-07/10. Role: Investigator. </li> <li>NIH-INBRE-Alaska "Investigations of Dynamics of Actin-binding Chicken Villin Headpiece Subdomain $25,000, 12/2010-11/2011 Role: PI.</li> <li>Instrumentation time award at Pacific Northwest National Laboratory, 06/2007-06/2008 ; 06/2009-06/2010. Role: PI. </li> <li>University of Alaska Faculty Development grants 2008, 2009, 2010. Role: PI.</li> <li>Environmental and Natural Resources Institute seed grant, 2011. Role: PI.</li> </div> </div> </body> </html>