Abstract
The ability of a polypeptide to fold into a unique, functional, three-dimensional structure in vivo is dependent upon its amino acid sequence and the function of molecular chaperone proteins and enzymes that catalyse folding. Intense study of the physical chemistry and cell biology of folding have greatly aided our understanding of the mechanisms normally employed. Evidence is accumulating that many disease-causing mutations and modifications exert their effects by altering protein folding. Here we discuss the pathobiology of these processes.
Original language | English (US) |
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Pages (from-to) | 456-459 |
Number of pages | 4 |
Journal | Trends in biochemical sciences |
Volume | 20 |
Issue number | 11 |
DOIs | |
State | Published - Nov 1995 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology