Membrane proteins not only represent a major class of drug targets, but have also become increasingly important in nanotechnology, biomimicry, and synthetic biology. A major focus in our lab is bacterial chemotaxis receptors, a key model system for understanding transmembrane signaling mechanisms. In the cell, chemotaxis proteins form remarkable nanoarrays that enable bacteria to sense the environment and move accordingly. Signaling by these complexes is thought to involve protein conformational changes, as well as changes in protein dynamics and disorder. Our approach is to integrate methods for assembly of native-like complexes with biophysical methods, including solid-state NMR and hydrogen exchange mass spectrometry (HDX-MS), to measure structure and dynamics and deduce the signaling mechanism. This work may enable the development of novel antibiotics targeting chemotaxis proteins and the ability to engineer bacteria for bioremediation and drug delivery.