Linked Life Data

1483409

Source:http://linkedlifedata.com/resource/pubmed/id/1483409

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1993-2-12
pubmed:abstractText
The secondary structure of a synthetic amyloid fragment des [Ala21,30]A42 was studied by circular dichroism and Fourier transformed infrared spectroscopy. Measurements were performed in trifluoroethanol/water and octyl beta-D-glucopyranoside solutions. The spectra of the peptide in trifluoroethanol indicate a high percentage of alpha-helical structure. However, in octyl glucoside, at and above the critical micelle concentration, the peptide adopts a beta-sheet conformation. Secondary structure analysis yields a predominant (> 70%) beta-sheet content. Our data suggest that the peptide backbone or polar side groups of des[Ala21,30]A42 interact with the sugar-coated surface of micelles, which promotes an alpha to beta conformational transition.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0175-7571
pubmed:author
pubmed:issnType
Print
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
345-8
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Conformational change of a synthetic amyloid analogue des[Ala21,30]A42 upon binding to octyl glucoside micelles.
pubmed:affiliation
Institute of Biophysics, Biological Research Center, Szeged, Hungary.
pubmed:publicationType
Journal Article, Comparative Study