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

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

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.

Detaljer

Författare
  • Maria Silow
  • Yee-Joo Tan
  • Alan R Fersht
  • Mikael Oliveberg
Enheter & grupper
Forskningsområden

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Biokemi och molekylärbiologi
Originalspråkengelska
Sidor (från-till)13006-13012
TidskriftBiochemistry
Volym38
Utgåva nummer40
StatusPublished - 1999
PublikationskategoriForskning
Peer review utfördJa