Knitting and snipping
Beteiligte Einrichtungen
Abstract
Hallmarks of proteins containing β-helices are their increased stability and rigidity and their aggregation prone folding pathways. While parallel β-helices fold independently, the folding and assembly of many triple β-helices depends on a registration signal in order to adopt the correct three-dimensional structure. In some cases this is a mere trimerization domain, in others specialized chaperones are required. Recently, the crystal structures of two classes of intramolecular chaperones of β-helical proteins have been determined. Both mediate the assembly of large tailspike proteins and release themselves after maturation; however, they differ substantially in their structure and autoproteolytic release mechanisms.
Bibliografische Daten
Originalsprache | Englisch |
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ISSN | 0959-440X |
DOIs | |
Status | Veröffentlicht - 04.2011 |
Anmerkungen des Dekanats
Copyright © 2011 Elsevier Ltd. All rights reserved.
PubMed | 21330133 |
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