Self Folded Tetrahedra as a Model of Protein Folding

• Mahogony Collins, Applied Molecular Biology & Biotechnology, University of Delaware

• John Jungck, Biological Sciences & Mathematical Sciences, University of Delaware

There are thousands of different proteins in the body that each have the ability to uniquely fold, in a matter of seconds. Proteins begin as linear sequences, consisting of hundreds to thousands of amino acids. Understanding how these different proteins can fold into a stable three dimensional structure so quickly, aids in making advancements in different biomedical and bioengineering disciplines. The main problem involved in folding speed is the Levinthal Paradox, which asks how the proteins are able to find a pathway that creates the folded structure as fast as possible. Another theory to consider is Ulam’s packing conjecture which states the hardest shape to pack would be a sphere, when compared to other 3D shapes. One method of visualizing the folded three dimensional structure of a protein is a tessellation of Delaunay tetrahedra whose vertices represent four interacting amino acids. In our lab, we use methods such as origami, the art of folding paper, and 4D printing 24 tetrahedra connected by hinges, both of these ideas can be tested. Once assembled, these linear tetrahedra can be manipulated to create spherical 3D shapes. Tetrahedra, a 4 sided pyramid, are a commonly found polyhedron in biological scenarios such as viral capsids. Using these naturally occurring shapes can aid in deepening the understanding of not only how proteins fold but also aid in making advanced biomedical tools or even improving self folding protective structures. By making macroscopic models, it is much easier to get a hands on and visual understanding of protein folding while using creative techniques.