Transient aggregates in protein folding are easily mistaken for folding intermediates.
It has been questioned recently whether populated intermediates are important for the protein folding process or are artefacts trapped in nonproductive pathways. We report here that the rapidly formed intermediate of the spliceosomal protein U1A is an off-pathway artefact caused by transient aggregation of denatured protein under native conditions. Transient aggregates are easily mistaken for structured monomers and could be a general problem in time-resolved folding studies.
Silow
M
M
Biochemistry, Chemical Centre, P.O. Box 124, S-221 00 Lund, Sweden.
Oliveberg
M
M
D016477:Artifacts; D002151:Calorimetry; D019791:Guanidine; D006146:Guanidines; D006801:Humans; D007700:Kinetics; D046911:Macromolecular Substances; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D010940:Plant Proteins; D011489:Protein Denaturation; D017510:Protein Folding; D016601:RNA-Binding Proteins; D017412:Ribonucleoprotein, U1 Small Nuclear / Q000737:chemistry* / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors / Q000737:chemistry / Q000378:metabolism; D017381:Spliceosomes / Q000378:metabolism
D006146:Guanidines; D046911:Macromolecular Substances; D010455:Peptides; D010940:Plant Proteins; D016601:RNA-Binding Proteins; D017412:Ribonucleoprotein, U1 Small Nuclear; D015842:Serine Proteinase Inhibitors; C075339:U1A protein; C093336:chymotrypsin inhibitor 2; D019791:Guanidine