Linked Life Data

16231928

Source:http://linkedlifedata.com/resource/pubmed/id/16231928

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
42
pubmed:dateCreated
2005-10-19
pubmed:abstractText
A force-spectroscopy-based approach is used to characterize separation between amyloidogenic peptide fragments of alpha-synuclein. Interactions between individual molecules are studied using a scanning-force-microscopy-based technique. Alpha-synuclein fragments are attached to the solid surfaces via flexible long poly-(ethylene glycol) linkers removing aggregation state uncertainty of solution-based approaches and spurious surface effects. Tethering one fragment to the scanning probe tip and another fragment to the second surface ensures that interactions between tethered molecules are studied. Control experiments with only one tethered peptide indicate peptide-peptide interactions as the source of observed interaction forces in the double-tether experiment. The temperature dependence of rupture forces from 17.5 degrees C to 40 degrees C reveals similar molecular parameters indicating that no significant conformational changes occur in the associated molecules over this temperature range. Rate-dependent measurements indicate conformational heterogeneity of joined peptide molecules.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0002-7863
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
127
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
14739-44
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Conformational heterogeneity of surface-grafted amyloidogenic fragments of alpha-synuclein dimers detected by atomic force microscopy.
pubmed:affiliation
Department of Chemistry, Duke University, Durham, North Carolina 27708, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't