Special Lecture

Seeing the invisible by Solution NMR Spectroscopy

Prof. Lewis Edward Kay

The research in Dr. Lewis E. Kay’s laboratory focuses on the development of NMR techniques for studying macromolecular structure and dynamics and the application of NMR techniques to problems of biological and clinical importance. In particular the research is divided into the following areas: 

1)  Methodological Developments.  Research is focused on developing 15N, 13C, 2H multi-dimensional NMR spectroscopy and gradient enhanced spectroscopy to increase the molecular weight limitations currently imposed on protein structure determination using conventional techniques.  A second area relates to the development of 15N and 13C relaxation techniques for the study of protein dynamics in solution.

  2)  Structural Studies of Proteins Involved in Signal Transduction.  In particular, they are studying the solution structures of molecules containing SH2 and SH3 domains from cytoplasmic tyrosine kinases.  A major goal is to understand in molecular terms the origin of the specificity of particular SH2-phosphotyrosyl peptide interactions. 

 3)  Protein Dynamics.  Methods are developed and applied to study backbone and sidechain protein dynamics and how dynamic properties change upon ligand binding or folding.  Relationships between dynamics and thermodynamics are being developed and applied to binding and folding events. 

4)  Protein Folding.  Methods are developed and applied to study protein folding, residual structure in unfolded and partially folded states and dynamic properties of these molecules.