Linked Life Data

8856062

Source:http://linkedlifedata.com/resource/pubmed/id/8856062

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1996-11-27
pubmed:abstractText
Local structures formed in early intermediates are thought to play a key role in orientating the protein folding pathway. Here, we test whether non-native interactions formed by eight N-terminal residues in early folding intermediates of tryptophan synthase beta chains [Navon, A., Schulze, A. J., Guillou, Y., Zylinksii, C. A., Baleux, F., Expert-Bezançon, N., Friguet, B., Djavadi-Ohaniance, L. & Goldberg, M. E. (1995) J. Biol. Chem. 270, 4255-4261] influence the folding kinetics. The kinetics of in vitro renaturation of wild-type beta chains and truncated beta chains lacking residues 2-9 were compared. Each step analyzed (molten globule formation, tryptophan shielding, closing up of distant residues, and complete renaturation) occurred with similar kinetics in the normal and truncated proteins. Thus, non-native interactions formed early during the folding of beta chains seem to influence neither the rate and efficiency of the complete renaturation, nor the kinetics of the early folding steps, which suggests that such non-native early intermediates are poorly stable and highly dynamic. This observation is consistent with the current view that productive folding should avoid the formation of stable intermediates.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
240
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
615-21
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Transient non-native interactions in early folding intermediates do not influence the folding kinetics of Escherichia coli tryptophan synthase beta 2 subunits.
pubmed:affiliation
Unité de Biochimie Cellulaire (CNRS URA 1129), Institut Pasteur, Paris, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't