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Protein folding is molecular origami. Proteins begin as disordered chains with specific sequences of amino acids. The specific sequence guides the chain to fold onto itself into a precise 3-d structure that then carries out the protein’s functional activities. Artwork by Mark Miller, Stowers Institute.

Mapping protein aggregation pathways in vivo. An empirical energy landscape describing aggregation of the human ALS-causing protein, TDP-43, in living cells. The landscape illustrates how finite oligomers compete with liquid-liquid phase separation, and the two types of assemblies go on to nucleate two very distinct forms of amyloid. On the X- and Y-axes are structural coordinates that distinguish different self-assembled states. On the Z-axis is the relative free energy of each state.

The nucleating interactome of the human death domain superfamily. Death domain-containing proteins are responsible for many of the decisions cells make in response to pathogens or damage, including the decision to die altruistically. How these proteins make these decisions involves interactions that trigger a cascade of self-templated aggregation. This heat map shows which death domains trigger such cascades for other death domains.

Modeling social behavior with yeast colonies. Two fluorescently labeled yeast strains with differing expression of a cell surface adhesin and surfactant protein, Flo11, (blue and green) demonstrate proximity-dependent fitness at the boundaries between the colors -- a beautiful example of metabolic competition and collaboration on nutrient-limited media.