Linked Life Data

2520771

Source:http://linkedlifedata.com/resource/pubmed/id/2520771

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1992-6-26
pubmed:abstractText
We have elucidated the X-ray diffraction structures of the psi[CH2NH] backbone-modified analogs of Z-Pro-Leu-Gly-NH2 and t-Boc-Pro-Leu-Gly-NH2 (N alpha-protected derivatives of the tripeptide amide representing the C-terminal tail of oxytocin) with the "reduced peptide bond" located at the Pro-Leu sequence. The comparative results of these pseudopeptides show that conformational properties are similar (i.e., C7 structure at the Pro), whereas the unmodified peptides diverge substantially (i.e., t-Boc-Pro-Leu-Gly-NH2 and H-Pro-Leu-Gly-NH2 each show type-II beta-bend at the Leu-Gly; and Z-Pro-Leu-Gly-NH2 shows an open folded structure). The results for t-Boc-Pro psi[CH2NH]Leu-Gly-NH2 represent the first unequivocal proof for the existence of a C7 structure in a linear peptide.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1040-5704
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
332-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Psi [CH2NH] backbone-modified peptides: first unequivocal observation of a C7 structure in a linear peptide.
pubmed:affiliation
Dept. of Organic Chemistry, University of Padova, Italy.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't