Formation of short-lived protein aggregates directly from the coil in two-state folding.
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.
Silow
M
M
Department of Biochemistry, Chemical Centre, Lund University, Sweden.
Tan
Y J
YJ
Fersht
A R
AR
Oliveberg
M
M
D002918:Chymotrypsin / Q000037:antagonists & inhibitors*; D001467:Hordeum / Q000737:chemistry; D006801:Humans; D007700:Kinetics; D010455:Peptides / Q000737:chemistry*; D010940:Plant Proteins; D017510:Protein Folding; D016601:RNA-Binding Proteins / Q000737:chemistry; D017412:Ribonucleoprotein, U1 Small Nuclear / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013329:Structure-Activity Relationship
D010455:Peptides; D010940:Plant Proteins; D016601:RNA-Binding Proteins; D017412:Ribonucleoprotein, U1 Small Nuclear; C075339:U1A protein; C093336:chymotrypsin inhibitor 2; D002918:Chymotrypsin