Design and characterization of natural and naturally-inspired helical protein assemblies Restricted; Files & ToC

Abstract

Protein helical assemblies are abundant in nature because they are useful to the cell and because they can form via a great diversity of mechanisms. In this work, multiple such assemblies are examined, from native-context A. tumefaciens T-pili to naturally derived CanA and Hyper2 proteins to ɑReps, which are naturally-inspired but rationally engineered. Nature has designed proteins that are extremely durable against thermal energy and enzymatic activity. Human scientists have developed predictive algorithms to make educated guesses about the tertiary and even quaternary structures of proteins. However, these powerful tools are primarily informed by proteins from organisms that either maintain their own body temperature (e.g., humans) or grow within animals that do (e.g., E. coli). The proteins described in this work do not always fully auto-assemble; instead, their assembly is mediated by lipids or divalent cations, or they are co-assemblies of multiple proteins. In other words, these modeling tools are very good at predicting how thermally unstable proteins fold. But hyperthermostable proteins such as those described in this paper are ostensibly better for designing tools. They are more likely to be correctly folded in a given condition and they will not degrade as quickly. For these reasons, study in thermostable proteins is as valuable as ever for protein design and structural biology in general.

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About this Dissertation

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School	Laney Graduate School
Department	Chemistry
Degree	Ph.D.
Submission	Dissertation
Language	English
Research Field	Biophysics, General Nanoscience Biology, Microbiology
Keyword	nanotube peptide nanotube alpharep cryo-EM structural biology pilus nanomaterial
Committee Chair / Thesis Advisor	Vincent Conticello, Emory University
Committee Members	Katherine Davis, Emory University Yonggang Ke, Emory University

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