Linked Life Data

19217080

Source:http://linkedlifedata.com/resource/pubmed/id/19217080

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2009-3-24
pubmed:abstractText
Ten C-glycosyl beta(2)- and beta/beta(2)-peptides with three to eight amino acid residues have been prepared. Solution and solid-phase peptide syntheses were employed to assemble beta(2)-amino acids in which C-glycosylic substituents are attached to the C-2 position of beta-amino acids. Conformational analysis of the C-glycosyl beta(2)-peptides using NMR and CD spectra indicates that the tripeptide can form a helical secondary structure. Besides, helix directions of the C-glycosyl beta/beta(2)-peptides are governed by the configuration at the alpha-carbon of the peptide backbone that originates from the stereocenter of the C-glycosyl beta(2)-amino acids.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1873-426X
pubmed:author
pubmed:issnType
Electronic
pubmed:day
31
pubmed:volume
344
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
613-26
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Preparation and conformational analysis of C-glycosyl beta(2)- and beta/beta(2)-peptides.
pubmed:affiliation
Department of Interdisciplinary Materials Science, Nara Women's University, Nara 630-8506, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't