The "correctly folded" state of proteins: Is it a metastable state?

Research output: Contribution to journalShort surveypeer-review


Alzheimer's disease, type H diabetes, Creutzfeldt-Jakob disease, and amyloid-related diseases: In each of these pathological situations, well-folded proteins undergo an irreversible transition from the "correctly folded" state to a collapsed β-sheet-rich structure. Here it is suggested that the aggregated form represents a global minimum in Gibbs energy for ensembles of protein molecules in general, and that at an infinite time any protein solution above a critical concentration will eventually undergo structural transition into the aggregated state.

Original languageEnglish
Pages (from-to)257-259
Number of pages3
JournalAngewandte Chemie - International Edition
Issue number2
StatePublished - 18 Jan 2002


  • Aggregation
  • Amyloidosis
  • Protein folding
  • Proteins


Dive into the research topics of 'The "correctly folded" state of proteins: Is it a metastable state?'. Together they form a unique fingerprint.

Cite this