A Study of the Effect of Amino Acid Substitutions on Cannula Mimetic Proteins Öffentlichkeit

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

About this Honors Thesis

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School	Emory College
Department	Chemistry
Degree	B.S.
Submission	Honors Thesis
Language	English
Research Field	Chemistry, Biochemistry Chemistry, Polymer
Stichwort	protein folding TEM supramolecular assembly
Committee Chair / Thesis Advisor	Vincent P. Conticello, Emory University
Committee Members	David Lynn, Emory University Katherine Davis, Emory University

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