Linked Life Data

17501917

Source:http://linkedlifedata.com/resource/pubmed/id/17501917

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
pubmed:issue
4
pubmed:dateCreated
2007-5-15
pubmed:abstractText
Some proteins are so much resistant to proteolysis and unfolding that they violate folding rules shared by the vast majority of proteins. These unusual proteins manage to fold into an active native conformation that is thermodynamically at best marginally, but often even less stable than the unfolded state. A huge energetic barrier traps these proteins kinetically in the folded state. The drawback of this situation is the need for a specialized chaperone that adds steric information to the proteins to cross this barrier on the folding pathway. Until now, our knowledge of these intriguing chaperones was restricted to the prodomains of secreted proteases, which function intramolecularly. Recent research has added more examples, which now include the membrane-anchored lipase-specific foldase and the pilus subunit specific chaperone, both acting intermolecularly. The case of the pilin chaperone is somewhat deviant in that steric information is definitely provided, but the pilus subunit adopts a thermodynamically favourable stable conformation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0950-382X
pubmed:author
pubmed:issnType
Print
pubmed:volume
64
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
917-22
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Chaperoning Anfinsen: the steric foldases.
pubmed:affiliation
Department of Molecular and Cellular Interactions, VIB and Department of Ultrastructure, Free University Brussels, Brussels, Belgium.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't