Source:http://linkedlifedata.com/resource/pubmed/id/10679622
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2000-3-21
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pubmed:abstractText |
We have investigated the conformational preferences of a newly synthesized C(alpha,alpha) symmetrically disubstituted glycine, namely alpha,alpha-dicyclopropylglycine (Dcp). We report here the crystal structure of a fully protected dipeptide containing Dcp, namely Z-Dcp(1)-Dcp(2)-OCH(3). Both Dcp residues are in a folded conformation. The overall peptide structural organization corresponds to an alpha-pleated sheet conformation, similar to that observed in linear peptides made up of alternating D- and L-residues and in Z-Aib-Aib-OCH(3) (Aib: alpha,alpha-dimethylglycine). These preliminary data suggest that the Dcp could represent an alternative as molecular tool to stabilize folded conformations.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-3525
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2000 John Wiley & Sons, Inc.
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pubmed:issnType |
Print
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pubmed:volume |
53
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
182-8
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pubmed:dateRevised |
2000-12-18
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pubmed:meshHeading | |
pubmed:year |
2000
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pubmed:articleTitle |
The crystal structure of a Dcp-containing peptide.
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pubmed:affiliation |
Centro Interuniversitario di Ricerca su Peptidi Bioattivi, di Biocristallografia, CNR, University of Napoli "Federico II," via Mezzocannone 4, I-80134 Napoli, Italy.
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pubmed:publicationType |
Journal Article
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