Linked Life Data

573753

Source:http://linkedlifedata.com/resource/pubmed/id/573753

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1979-12-27
pubmed:abstractText
The addicting properties of [Leu5]enkephalin in mice are conserved in the LSer3 analogue and lost both in the L-Ser2 analogue and in all the L-Cha4 derivatives of the above peptides. Fluorescence measurements in water show the presence of hydrogen-bonded tyrosul OH groups in [Leu5]-enkephalin and in its LSer2 analogue. The Phe4/Cha replacements do not influence these equilibria, but they affect the near u.v. dichroism of the hydrogen bonded tyrosyl residues. In the peptide absorption region in water solution, only [Leu5]-enkephalin and its cyclohexylalnyl derivative show a positive dichroism towards high frequencies, which is maintained in 8 M ura. No clear relation is found between conformation(s) in solution and biological activity. A II' beta-turn, with residues in positions 2 and 3 at the corners, is suggested for the conformation of enkephalin bound to the receptors involved in the bioassay here used.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0367-8377
pubmed:author
pubmed:issnType
Print
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
34-40
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Synthetic enkephalins. Addicting properties and conformational studies in solution.
pubmed:publicationType
Journal Article