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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1997-9-23
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pubmed:abstractText |
The terminally blocked tetrapeptide pBrBz-[D-(alpha Me)Leu]2-D-(alpha Me)Val-D-(alpha Me)Leu-OfBu is folded in the crystal state in a left-handed 3(10)-helical structure stabilized by two consecutive 1<--4 C = O...H-N intramolecular H-bonds, as determined by X-ray diffraction analysis. A CD study strongly supports the view that this conformation is also that largely prevailing in MeOH solution. A comparison with the published conformation of pBrBz-[D-(alpha Me)Leu]4-OfBu indicates that incorporation of a single internal beta-branched (alpha Me)Val guest residue into the host homo-tetrapeptide from the gamma-branched (alpha Me)Leu residue is responsible for a dramatic structural perturbation, i.e. an inversion of the 3(10) screw sense from right to left-handed.
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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:issn |
1075-2617
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
396-402
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9223019-Amino Acid Sequence,
pubmed-meshheading:9223019-Circular Dichroism,
pubmed-meshheading:9223019-Crystallography, X-Ray,
pubmed-meshheading:9223019-Hydrogen Bonding,
pubmed-meshheading:9223019-Methylation,
pubmed-meshheading:9223019-Models, Molecular,
pubmed-meshheading:9223019-Molecular Structure,
pubmed-meshheading:9223019-Oligopeptides,
pubmed-meshheading:9223019-Protein Folding,
pubmed-meshheading:9223019-Protein Structure, Secondary
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pubmed:articleTitle |
Inversion of 3(10)-helix screw sense in a (D-alpha Me)Leu homo-tetrapeptide induced by a guest D-(alpha Me)Val residue.
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pubmed:affiliation |
Department of Organic Chemistry, University of Padova, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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