Linked Life Data

21797254

Source:http://linkedlifedata.com/resource/pubmed/id/21797254

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
35
pubmed:dateCreated
2011-8-30
pubmed:abstractText
The interplay of modern molecular simulation and high-quality nuclear magnetic resonance (NMR) experiments has reached a fruitful stage for quantitative characterization of structural ensembles of disordered peptides. Amyloid-? 1-42 (A?42), the primary peptide associated with Alzheimer's disease, and fragments such as A?21-30 are both classified as intrinsically disordered peptides (IDPs). We use a variety of NMR observables to validate de novo molecular dynamics simulations in explicit water to characterize the tertiary structure ensemble of A?42 and A?21-30 from the perspective of their classification as IDPs. Unlike the A?21-30 fragment that conforms to expectations of an IDP that is primarily extended, we find that A?42 samples conformations reflecting all possible secondary structure categories and spans the range of IDP classifications from collapsed structured states to highly extended conformations, making it an IDP with a far more heterogeneous tertiary ensemble.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1520-4995
pubmed:author
pubmed:issnType
Electronic
pubmed:day
6
pubmed:volume
50
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7612-28
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Homogeneous and heterogeneous tertiary structure ensembles of amyloid-? peptides.
pubmed:affiliation
Graduate Group in Biophysics, University of California, Berkeley, California 94720, United States.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, N.I.H., Extramural