INBRE
INBRE

Liliya Vugmeyster

Assistant Professor

Department of Chemistry
Faculty Fellow, Environmental and Natural Resources Institute
University of Alaska Anchorage
aflv@uaa.alaska.edu 
phone (907)-786-4709
http://aflv.uaa.alaska.edu/ 

● Biochemistry   ● Cell Biology

Affiliations
● INBRE
   (IDeA Network of Biomedical Research Excellence)
● University of Alaska Anchorage
   Department of Biological Sciences
 
Specialties
● Chemistry
 
Research Overview
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. 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.

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.

Peer Reviewed Publications (in chronolgical order)

1. 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.

2. 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.

3.  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.

4. 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.

5.  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.

6.  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.

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, Bodenhausen G, Appl Magn Reson 28, 147-163 (2005) Temperature dependent protein backbone dynamics from auto- and cross-correlated NMR relaxation rates.

9. 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.

10. Vugmeyster L, McKnight CJ, J Biomol NMR 43, 39-50 (2009) Phosphorylation-induced changes in backbone dynamics of dematin headpiece C-terminal subdomain [

11. 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 [PMID: 19479944] 

12.   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 [PMID: 19652835]

13.   Vugmeyster L, Ostrovsky D, Ford JJ, Burton SD, Lipton AS, Hoatson GL, Vold RL, J. Am. Chem. Soc. 131 (38), 13651–13658 (2009) Probing the dynamics of a protein hydrophobic core by deuteron solid-state nuclear magnetic resonance spectroscopy [PMID: 19772361] 

14.  Vugmeyster L, Ostrovsky D, Ford JJ, Lipton AS, J. Am. Chem. Soc. 132 (12), 4038–4039 (2010) Freezing of dynamics of a methyl group in a protein hydrophobic core at cryogenic temperatures by deuteron NMR spectroscopy. 

15.   Vugmeyster L, Ostrovsky D, Li Y, J. Biomol. NMR 47 (2), 155-162 (2010) Comparison of fast backbone dynamics at amide nitrogen and carbonyl sites In dematin headpiece C-terminal domain and Its S74E mutant [PMID: 20201523]

16.   Vugmeyster L, Ostrovsky D, Moses M, Ford JJ, Lipton AS, Hoatson GL, Vold RL, J. Phys. Chem. 114 (48), 15799–15807 (2010) 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 [PMID: 21077644]

17.  Vugmeyster L, Ostrovsky D, J. Biomol. NMR, 50(2), 119-127 (2011) Temperature Dependence of Fast Carbonyl Backbone Dynamics in Chicken Villin Headpiece Subdomain [PMID: 21416162] 

18.  Vugmeyster L, Ostrovsky D, Khadjinova A, Ellden J, Hoatson GL, Vold RL, Biochemistry (2011), 50 (49), 110637-10646 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 [PMID: 22085262]

19.  Vugmeyster L, Ostrovsky D, Hoatson GL, Vold RL,  (2012) Glassy Dynamics of Methyl groups in Chicken Villin Headpiece Subdomain Protein Revealed by Deuteron NMR relaxation (Submitted to J. Phys. Chem 2012)

20.  Vugmeyster L, Do T, Ostrovsky D, Fu R, Hagedorn B, submitted to Solid State NMR(2012) Characterization of Water Dynamics in Frozen Soils by Solid-State Deuteron NMR [PMID:  22578873]