Nuclear Magnetic Resonance NMR-based Structural Biology Research

Our laboratory specializes in nuclear magnetic resonance (NMR)-based structural biology research. We are particularly interested in understanding the crucial links between the molecular structures, internal dynamics, and biochemical functions of proteins that are of importance to human endeavors. Questions of interest are: What is the connection between a protein’s three-dimensional architecture, flexibility of its amino acids and of its structural elements, and its biological function(s)? How do atomic structures and internal dynamics modulate the biochemical activity of proteins? What is the significance of conserved amino acid residues in protein families? Our approach to providing answers to these scientific issues is to use modern multidimensional (2D, 3D, 4D), heteronuclear (¹H, ¹⁵N, ¹³C, ²H) solution nuclear magnetic resonance (NMR) spectroscopy in conjunction with complementary biophysical techniques. We are currently investigating the structural and functional properties of several intriguing proteins.

Our Thermal Biology-related research is focused on the characterization of extremophilic proteins from microorganisms existing in the thermal environments in Yellowstone National Park. 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 “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 thermodynamical characteristics (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 genomics research taking place within TBI.

Current Laboratory Personnel:

Anupam Goel: Ph.D. Student
Emilio Reyes, Ph.D. Student
Casey Schlenker, Ph.D. Student
Haley Arthun, Undergraduate Student
Woody Cranston, Technical Support Staff

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