Linked Life Data

7575574

Source:http://linkedlifedata.com/resource/pubmed/id/7575574

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1995-11-2
pubmed:abstractText
Using CD spectroscopy we have investigated the effect of Cu2+ on the secondary structure of synthetic peptides Octa4 and Hexa4 corresponding to tetra-repeats of the octapeptide of mammalian PrP and the hexapeptide of chicken PrP. In addition, fluorescence spectroscopy was used to estimate the dissociation constants (Kd), of Cu2+ binding by both peptides. Both peptides exhibited unusual CD spectra, complicated by the high proportion of aromatic residues, revealing little secondary structure in aqueous solution. Addition of Cu2+ to Hexa4 induced an increase in random coil to resemble Octa4. The fluorescence of both peptides was quenched by Cu2+ and this was used to calculate Kd's of 6.7 microM for Octa4 and 4.5 microM for Hexa4. Other divalent cations showed lesser effects on the fluorescence of the peptides.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
214
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
993-9
pubmed:dateRevised
2010-8-25
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein: structural studies using synthetic peptides.
pubmed:affiliation
MRC Neurochemical Pathology Unit, Newcastle General Hospital, Newcastle upon Tyne, United Kingdom.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't