Dr. Liliya Vugmeyster
Assistant Professor Chemistry
Dr. Vugmeyster's home page
Dynamics and folding of proteins using solution and solid-state nuclear magnetic resonance techniques and theoretical/computational approaches.
Current Research Projects
1) Dynamics of hydrophobic cores by deuteron solid-state NMR spectroscopy and computational modeling.
2) Backbone dynamics of headpiece proteins studied by hetero-nuclei solution NMR techniques.
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 in a variety of 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.