Linked Life Data

15999178

Source:http://linkedlifedata.com/resource/pubmed/id/15999178

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
2005-7-6
pubmed:abstractText
Here we introduce a peptide model based on an alpha-helical coiled coil peptide, providing a simple system which can be used for a systematic study of the impact of different metal ions in different oxidation states on peptide secondary structure on a molecular level; histidine residues were incorporated into the heptad repeat to generate possible complexation sites for Cu2+ and Zn2+ ions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1477-0520
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2500-2
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
From alpha-helix to beta-sheet--a reversible metal ion induced peptide secondary structure switch.
pubmed:affiliation
Freie Universität Berlin, Institut für Chemie, Organische Chemie, Takustrasse 3, 14195 Berlin, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't