The amide proton resonances can be exploited in a number of ways to monitor the structure and dynamics of the protein. We are especially interested in defining the folding pathway of the protein in both an energetic and a k inetic sense. The second area of interest is the phenomenon of chemotaxis in bacteria. The bacteria sense temporal changes in the concentration of attractan t or repellent molecules and change their swimming behavior accordingly. This process requires sensing the concentrations of attractant or repellent, the behavioral response to rapid changes in these concentrations, and the relatively slow adaptation to new concentrations which r eturns the swimming behavior to the unstimulated condition.
Adaptation is associated with the reversible methylation of four transmembrane receptors.
These proteins receive environmental information from outside the membrane and transmit that information to the cytoplasm. We are interested in defining how environmental information is transmitted across the inner membrane and how that information is used to allow behavioral adaptation. The open circles represent the amide nitrogen atoms of the active site residues. Bertelsen, E.B., G.C. Flynn, and F.W. Dahlquist. Topology and Dynamics of the 10 kDa C-terminal Domain of DNAK in Solution.