Research Projects

B. NMR-based structural and dynamical analysis of small thermostable proteins originating from Sulfolobus spindle shaped virus-1 (SSV-1)

We have also become very interested in proteins originating from organisms living in the hot and acidic thermal pool of Yellowstone National Park. This research is part of MSU's Thermobiology Institute (TBI). A research theme that is particularly attractive to us is: What are the characteristic molecular features of proteins originating from thermophilic organisms that distinguish them from their mesophilic partners?
For example, how do organisms adapt to the high temperature (T > 70 oC) , acidic (pH < 4.0), and a toxic metal-rich (arsenic, iron, copper, mercury, and others) environment of YNP thermal pools? How do proteins originating from extremophiles get modified to function in such an environmental context? What changes take place at the molecular levels? How do proteins modify their thermodynamic properties (i.e. thermal stability, flexibility of functional residues) to operate efficiently in thermophilic conditions? How do proteins cope with arsenic, cadmium, or copper-rich environments? Modern multidimensional, heteronuclear (1H, 15N, 13C, 2H) solution nuclear magnetic resonance (NMR) spectroscopy is an excellent technique to provide answers to these fundamental issues, both at the structural and motional levels of atoms, and complements well the X-ray-based structural biology research programs taking place within TBI.

Publications

Lara Taubner, Michelle McGuirl, David Dooley, and Valerié Copié, "¹H, ¹³C, ¹⁵N backbone and sidechain resonance assignments for the 18 kDa apo-NosL, a novel copper(I) containing protein from Achromobacter Cycloclastes." A. Letter to the Editor: Journal of Biomolecular NMR. Vol 29, pp. 211-212 (2004)

Personnel:
Valérie Copié

Keywords:
NMR, Protein Chemistry, Structure

Return to regular view	Text-only	Updated: 11/6/09