Linked Life Data

17761149

Source:http://linkedlifedata.com/resource/pubmed/id/17761149

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2007-9-11
pubmed:abstractText
Transthyretin (TTR) is an amyloidogenic protein involved in many mental diseases. The peptide derived from TTR (105-115) has been widely studied as a model peptide for understanding the mechanism of amyloid fibril formation. However, the detailed arrangement of this peptide in amyloid fibril is still unclear. We have studied the amyloid fibril formation process of TTR (105-115) by introducing a pair of FRET probes into the peptide with a dansyl group at the N-terminal and a tryptophan residue at the C-terminal. Our experiment demonstrated that the strands of TTR (105-115) in the same beta-sheet may be parallel and the mating sheets may be anti-parallel to each other in the amyloid fibril. The kinetics followed by FRET and EM indicated for a possible intermediate state and the distance between sheets became shorter when the intermediate amyloid fibril turns into a more matured form.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
362
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
689-94
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Detecting the inter-peptide arrangement and maturation process of transthyretin (105-115) amyloid fibril using a FRET pair with short Förster distance.
pubmed:affiliation
Beijing National Laboratory for Molecular Sciences, State Key Laboratory of Structural Chemistry for Unstable and Stable Species, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't