Linked Life Data

11536844

Source:http://linkedlifedata.com/resource/pubmed/id/11536844

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5-6
pubmed:dateCreated
1999-4-25
pubmed:abstractText
Sequential oligo- and polypeptides based on glutamic acid and leucine residues have been synthesized. In pure water, they exhibit a random coil conformation. Addition of very small amounts of divalent metallic cations induces the formation of ordered structure in the peptides which remain in solution. Higher salt concentrations precipitate the peptides. Polypeptides with alternating glutamic acid and leucine residues undergo a coil to beta-sheet transition in the presence of Ca2+, Ba2+, Mn2+, Co2+, Zn2+ and Hg2+. Addition of Cu2+ or Fe3+ induces the formation of an alpha-helix. Solid amorphous CdS generates water soluble beta-sheets, as well. Sequential poly(Leu-Glu-Glu-Leu) adopts an alpha-helix in the presence of divalent cations. The sequence-dependent conformational diversity was extended to poly(Asp-Leu) and poly(Leu-Asp-Asp-Leu).
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
S
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0169-6149
pubmed:author
pubmed:issnType
Print
pubmed:volume
27
pubmed:owner
NASA
pubmed:authorsComplete
Y
pubmed:pagination
585-95
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Conformational variety of polyanionic peptides at low salt concentrations.
pubmed:affiliation
Centre de Biophysique Moleculaire, Orleans, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't