Physical Chemistry of Biological Free Energy Transduction As Demonstrated by Elastic Protein-Based Polymers†

TLDR: This article presents a general mechanism for protein folding and function and demonstrates the mechanism by designing model proteins capable of performing many of the energy conversions that sustain life and by designing diverse biomolecular machines and materials with promising applications for society.

Abstract: This article, on protein-based polymers comprised of repeating peptide sequences, reviews studies from the author's laboratory covering a period of more than two decades; it presents a general mechanism for protein folding and function and demonstrates the mechanism by designing model proteins capable of performing many of the energy conversions that sustain life and by designing diverse biomolecular machines and materials with promising applications for society. All polymers with the correct balance of apolar and polar moieties, including water soluble proteins and protein-based polymers, increase order by a hydrophobic folding and assembly transition as the temperature is raised above a critical onset temperature, designated as Tt. Instead of varying the temperature, however, innumerable variables lower the value of Tt from above to below the operating temperature to drive folding and function. Thus, this inverse temperature transition provides a fundamental mechanism whereby proteins fold and function ...