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Understanding how signal inputs and outputs are organised in membrane protein signalling networks is an important question in biology. The current goal is to derive methods that would allow the 'watching' of these network proteins in action and at atomic resolution to see details of their structure. This requires the addition of a 'time' dimension to structural biology so that the spatio-temporal parameters of all atoms in each protein can be described in detail. This is a huge challenge that in cell-free systems has begun to be partially addressed through dynamic experiments combined with molecular simulations. However, in cells, the functions of particular structural motifs are not just constrained by Brownian motions, energy landscapes and thermodynamics, but also by the local availability of partners in subcellular compartments and the boundary constraints imposed by cell environments, for example in the plasma membrane, with its 2D dimensionality, local curvature and electric fields. To understand protein function in cells, observations have to be made in the only physiologically-relevant 'laboratory', the cell. This adds levels of complexity to an already vast challenge.

Investigating the Conformation of HER Membrane Proteins in Cells via Single Molecule and FLIM Microscopy