These resonances can be exploited in a number of ways to monitor the structure and dynamics of the protein. The laboratory is especially interested in defining the folding pathway of the protein in both an energetic and a kinetic sense. T he second major area of interest is the phenomenon of chemotaxis in bacteria. The bacteria sense temporal changes in the concentration of attractant or repellent molecules and change their swimming behavior accordingly. This process requires sensing the concentrations of attractant or repellent, behavioral response to rapid changes in these concentrations and relatively slow adaptation to the new concentrations, which returns 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. The interests of the laboratory are in defining how environmental information is transmitted across the inner membrane and how that information is used to allow behavioral adaptation. Structural analysis using NMR and x-ray diffraction methods play a major role in this work. The open circles represent the amide nitrogen atoms of the active site residues.