Linked Life Data

19236027

Source:http://linkedlifedata.com/resource/pubmed/id/19236027

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2009-3-12
pubmed:abstractText
In this work, we report molecular dynamics simulations on a fragment of the human prion protein spanning residues 31-120, with copper(II) bound to the repeat region in several ways corresponding to the known intra- and inter-repeat coordination modes, or to the metal site located at His111. The results of this study point to a different structuring tendency of the protein fragment depending on copper binding mode, with the highest degree of structuring in the case of intrarepeat Cu(II) coordination corresponding to high copper concentration.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1520-6106
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
113
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3277-9
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Molecular dynamics study of the Cu2+ binding-induced "structuring" of the N-terminal domain of human prion protein.
pubmed:publicationType
Letter, Research Support, Non-U.S. Gov't