Abstract
The ability of long polypeptide chains to form correctly folded and functional proteins in the intracellular environment is a complex process, requiring participation of other protein components and biased native-like interactions between residues. Failure to fold correctly can lead to a variety of disease states, in which proteins are deposited in highly organized aggregates or are degraded in the proteasome. Examples of the former are the amyloidoses, such as Alzheimer’s disease (AD) and the spongioform encephalopathies, whereas in cystic fibrosis (CF) and some forms of nephrogenic diabetes insipidus, relevant misfolded protein molecules are degraded. Cell-free protein synthesis is used to examine gene expression, membrane insertion into microsomes or mitochondria, early endoplasmic reticulum (ER) folding events, exclusion mechanisms for misfolded proteins, effects of protein synthesis inhibitors, and even for the production of microgram quantities of proteins.
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Cuthbert, A.W., Fuller, W. (2003). Investigation of Folding and Degradation of In Vitro Synthesized Mutant Proteins in Microsomes. In: Bross, P., Gregersen, N. (eds) Protein Misfolding and Disease. Methods in Molecular Biology™, vol 232. Humana Press. https://doi.org/10.1385/1-59259-394-1:265
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DOI: https://doi.org/10.1385/1-59259-394-1:265
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