Formation of Short-Lived Protein Aggregates Directly from the Coil in Two-State Folding

Research output: Contribution to journalArticle

Abstract

Recent results on the 102 residue protein U1A show that protein aggregation is not always slow and irreversible but may take place transiently in refolding studies on a millisecond time scale. In this study we observe a similar aggregation behavior with the classical two-state protein CI2. Since both U1A and CI2 appear to fold directly from the coil at low protein concentrations, it is likely that the aggregates also form directly from the coil. This is in contrast to the behavior of larger multistate proteins where aggregation occurs in connection to "sticky" intermediates.

Details

Authors
  • Maria Silow
  • Yee-Joo Tan
  • Alan R Fersht
  • Mikael Oliveberg
Organisations
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Biochemistry and Molecular Biology
Original languageEnglish
Pages (from-to)13006-13012
JournalBiochemistry
Volume38
Issue number40
Publication statusPublished - 1999
Publication categoryResearch
Peer-reviewedYes