TEACHING

Classes taught:
General Chemistry, Concepts in Chemistry, Survey of Chemistry, Survey of Chemistry Laboratory
Physical Chemistry, Physical Chemistry Laboratory.

Current teaching goals: 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.

EDUCATION

Ph. D. in Chemistry, 2001

State University of New York at Stony Brook, NY
Title of thesis: Studies in protein folding and dynamics using magnetic resonance spectroscopy.
Thesis supervisors: Prof. Daniel P. Raleigh, SUNY at Stony Brook,
Prof. Arthur G. Palmer, Columbia University.

B.S. in Chemistry, 1996

Lehman College, City University of New York NY

RESEARCH INTERESTS

Dynamics and folding of proteins using solution and solid-state nuclear magnetic resonance techniques and theoretical/computational approaches.

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.

Shapes/structures of proteins are not static – these molecules “breathe" and their structures fluctuate. These fluctuations have been related to biological functions that these molecules are responsible for. The goal of my studies is to investigate the dynamics of proteins on various time scales and at various conditions: in solution and solids phases, at temperatures from 10K to 300K.

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^-9sec) 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.

COLLABORATORS

• Robert L. Vold, College of William and Mary
• James C. McKnight, Boston University School of Medicine
• Arthur G. Palmer, Columbia University
• Sarah Burton, Joseph Ford, Andrew Lipton, Pacific Northwest National Laboratory
• Dmitry Ostrovsky, University of Alaska Anchorage

PROFESSIONAL EXPERIENCE

Current Position:

Assistant Professor, Department of Chemistry, University of Alaska Anchorage

Visiting Scientist:

February-August2006
Boston University School of Medicine, Boston, MA
Laboratory of Prof. James McKnight

Postdoctoral Position:

September 2004-December 2005
Laboratory of Prof. Judith Herzfeld
Brandeis University,
Waltham MA

Visiting Scientist Position:

September 2004-August 2005
Laboratory of Prof. Robert Griffin
Francis Bitter Magnet Laboratory
Massachusetts Institute of Technology,
Cambridge MA

Postdoctoral Position:

2002 – 2004
Postdoctoral fellow in the laboratory of Prof. Geoffrey Bodenhausen
Ecole Polytechnique Fédérale de Lausanne, Switzerland.

LIST OF PUBLICATIONS

1. Vold RL, Hoatson GL, Vugmeyster L, Ostrovsky D, DeCasto PJ, Phys. Chem. Chem. Phys. 11, 7008-7012 (2009) Solid State Deuteron Relaxation Time Anisotropy Measured With Multiple Echo Acquisition.  
2. Vugmeyster L Magn. Reson. Chem. 47, 746-751 (2009) Slow Backbone Dynamics of Chicken Villin Headpiece Subdomain Probed by NMR C?-N Cross-Correlated Relaxation.  
3. Vugmeyster L, Ostrovsky D, Ford JJ, Burton SD, Lipton AS, Hoatson GL, Vold RL, accepted to J. Am. Chem. Soc. ASAP (web) DOI: 10.1021/ja902977u (2009) Probing the Dynamics of a Protein Hydrophobic Core by Deuteron Solid-State Nuclear Magnetic Resonance Spectroscopy.  
4. Vugmeyster L, McKnight CJ, J Biomol NMR 43, 39-50 (2009) Phosphorylation-induced changes in backbone dynamics of dematin headpiece C-terminal subdomain.
5. Vugmeyster L, McKnight CJ, Biophys J 95, 5941-5960 (2008) Slow Motions in Chicken Villin Headpiece Subdomain Probed by Cross-correlated NMR Relaxation of Amide NH Bonds in Successive Residues.
6. Vugmeyster L, Bodenhausen G, Appl Magn Reson 28, 147-163 (2005) Temperature dependent protein backbone dynamics from auto- and cross-correlated NMR relaxation rates.
7. Vugmeyster L, Perazzolo C, Wist J, Frueh D, Bodenhausen G, J Biomol NMR 28, (2), 173-177 (2004) Evidence of slow motions by cross-correlated chemical shift modulation in deuterated and protonated proteins.
8. Vugmeyster L, Pelupessy P, Vugmeister BE, Abergel D, Bodenhausen G, Comptes Rendus de l'Académie des Sciences (section de Physique) 5 (3), 377-386 (2004) Cross-correlated relaxation in NMR of macromolecules in the presence of fast and slow dynamics.
9. Wang M, Tang Y, Sato S, Vugmeyster L, McKnight CJ, Raleigh DP, J Am Chem Soc 125 (20), 6032-6033 (2003) Dynamic NMR lineshape analysis demonstrates that the Villin Headpiece Domain folds on the microsecond time scale.
10. Vugmeyster L, Raleigh DP, Palmer AG, Vugmeister BE, J Am Chem Soc 125 (27), 8400-8404 (2003) Beyond the decoupling approximation in the model free approach for the interpretation of NMR relaxation of macromolecules in solution.
11. Vugmeyster L, Trott O, McKnight CJ, Raleigh DP, Palmer AG, J Mol Biol, 320 (4), 841-854 (2002) Temperature-dependent dynamics of the villin headpiece helical subdomain, an unusually small thermostable protein.
12. Vugmeyster L, Kroenke CD, Picart F, Palmer AG, Raleigh DP, J Am Chem Soc , 122 (22), 5387-5388 (2000) N15 R1rho measurements allow the determination of ultrafast protein folding rates.
13. Vugmeyster L, Kuhlman B, Raleigh DP, Protein Science, 7 (9), 1994-1997 (1998) 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.