The native folded state of a protein is directly encoded in its amino acid sequence. Proteins typically adopt a fold that represents the lowest energy state for that sequence of amino acids. While there may be a single lowest energy state for a particular protein, the primary sequence can take any number of paths to arrive at this most thermodynamically stable fold. In the process of folding a protein, the amino acid sequence samples a subset of these conformations as it proceeds from a high free energy to a low free energy state. Although the final stable structure is directly encoded in the amino acid sequence, molecular chaperones can partially unfold proteins to allow them to better sample the conformational landscape. We can use an energy landscape funnel as a way to visualize the various pathways a given amino acid sequence may take to achieve its final folded state.