143 Scopus citations


Amyloid formation typically follows a time course in which there is a long lag period followed by a rapid formation of fibrils. In this review, I show that the standard mechanisms of polymerization need to be expanded to consider that the monomeric proteins/peptides involved in amyloid formation are intrinsically disordered and exist as an ensemble of disordered-collapsed states. The review focuses primarily on events which occur in the long lag period defining these as protein folding issues, coupled with formation of oligomers. Experimental methods to explore folding and oligomerization issues over a wide range of protein concentrations using primarily fluorescence and 19F-NMR methods are discussed. Published by Cold Spring Harbor Laboratory Press.

Original languageEnglish
Pages (from-to)2334-2344
Number of pages11
JournalProtein Science
Issue number11
StatePublished - Nov 2007


  • Fluorescence spectroscopy
  • Intrinsically disordered proteins
  • NMR
  • Nucleation
  • Oligomers
  • Polymerization


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