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 aggrega...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1997-06, Vol.94 (12), p.6084-6086
Hauptverfasser:	Silow, Maria, Oliveberg, Mikael
Format:	Artikel
Sprache:	eng
Schlagworte:	Aggregation Aggregation artefacts Biochemistry Biologi Biological Sciences Calorimetry Guanidine Guanidines Humans Kinetics Macromolecular Substances Monomers Natural Sciences Naturvetenskap Off-pathway intermediates Peptides - chemistry Peptides - metabolism Plant Proteins Protein Denaturation Protein Folding Protein refolding Proteins Ribonucleoprotein, U1 Small Nuclear - chemistry Ribonucleoprotein, U1 Small Nuclear - metabolism RNA-Binding Proteins Serine Proteinase Inhibitors - chemistry Serine Proteinase Inhibitors - metabolism Spliceosomes - metabolism U1A spliceosomal protein
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Beschreibung
Zusammenfassung:	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.
ISSN:	0027-8424 1091-6490 1091-6490
DOI:	10.1073/pnas.94.12.6084