Defective protein folding as a basis of human disease

Philip J. Thomas, Bao He Qu, Peter L. Pedersen

Research output: Contribution to journalReview article

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 languageEnglish (US)
Pages (from-to)456-459
Number of pages4
JournalTrends in biochemical sciences
Volume20
Issue number11
DOIs
StatePublished - Nov 1995

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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