Abstract
Protein assemblies and self-assembling peptides are finding new and diverse ways to be implemented in various fields of science. Previous research has presented the discovery of protein assemblies and self-assembling peptides throughout nature and the various roles they have in their environments. As more is understood about how they function and what properties contribute to that level of functioning, the application of these proteins becomes more diverse. We studied the structures of supramolecular assemblies from the archaea extremophile P. abyssi to better understand its use of strand donation polymerization, the ability to form Cannula A and Cannula B nanotubes with high heat and the presence of calcium, and how residue substitutions affect the overall process. The role that ligands and amino acid residues play in the lateral association of these cannulae is not yet completely known, but substituting residues of Cannula B to create a higher similarity to that of Cannula A led to greater polymerization under less strict conditions.
Table of Contents
Introduction Materials and Methods Plasmid DNA isolation and purification Protein expression Transformation protocol Protein isolation and purification Assembly conditions Sample assembly preparation Circular dichroism (CD) spectroscopy Transmission electron microscopy (TEM) Results and Discussions Secondary Structure Characterization Supramolecular Assemblies Conclusion and Future Directions Supplemental Information
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