Taking charge of proteins from neurodegeneration to industrial biotechnology.

Advances in Protein Chemistry and Structural Biology
Bryan F ShawKym F Faull

Abstract

The aggregation and precipitation of a soluble protein-within a motor neuron, or a pharmaceutical vial, or even inside a industrial-scale hydrolysis chamber-is a problem in human health and in biotechnology. A growing body of research is suggesting that the magnitude of the net charge of a protein is a determinant of the rate at which proteins self-assemble in solution into aggregates with amorphous or fibrillar (or uncharacterized) morphologies. This chapter discusses how this apparently simple electrostatic effect might explain-in part or entirely-the pathogenicity of some mutations that cause familial protein aggregation diseases-especially the familial forms of amyotrophic lateral sclerosis that are caused by mutations in the gene encoding superoxide dismutase-1 (SOD1). In parallel, this chapter also discusses how understanding these electrostatic effects can guide the engineering of industrial enzymes (such as alpha-amylase from Bacillus licheniformis) into forms that are more resistant to aggregation and thermal precipitation than the enzymes that are currently used, for example, in the production of ethanol from starch or cellulose.

Citations

Jun 17, 2016·Biochemistry·Casper HøjgaardJakob R Winther
Sep 6, 2012·International Journal of Molecular Sciences·Seong Il ChoiBaik L Seong
Jun 14, 2012·Protein Science : a Publication of the Protein Society·Yunhua ShiBryan F Shaw
Feb 20, 2019·Chemistry : a European Journal·Collin T Zahler, Bryan F Shaw
Nov 26, 2019·Quarterly Reviews of Biophysics·Gareth S A WrightS Samar Hasnain
Oct 25, 2016·FEBS Letters·Hiroki JozawaYutaka Kuroda
Apr 26, 2021·Journal of Evolutionary Biology·Ran TianGuang Yang

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