Source:http://linkedlifedata.com/resource/pubmed/id/11786606
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5558
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pubmed:dateCreated |
2002-2-15
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pubmed:abstractText |
Differences in the two-dimensional packing arrangements of racemic and enantiomeric crystalline self-assemblies on the water surface of amphiphilic activated analogs of lysine and glutamic acid have been used to prepare oligopeptides of homochiral sequence and oligopeptides of single handedness from chiral nonracemic mixtures. The crystalline structures on the water surface were determined by grazing incidence x-ray diffraction and the diastereomeric composition of the oligopeptides by matrix-assisted laser desorption time-of-flight mass spectrometry with enantio-labeling. These results suggest that reactivity of ordered clusters at interfaces might have played a role in the generation of early homochiral biopolymers.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Biopolymers,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Water
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1095-9203
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
295
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1266-9
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pubmed:dateRevised |
2007-3-19
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pubmed:meshHeading |
pubmed-meshheading:11786606-Biopolymers,
pubmed-meshheading:11786606-Crystallization,
pubmed-meshheading:11786606-Glutamic Acid,
pubmed-meshheading:11786606-Lysine,
pubmed-meshheading:11786606-Oligopeptides,
pubmed-meshheading:11786606-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:11786606-Stereoisomerism,
pubmed-meshheading:11786606-Water,
pubmed-meshheading:11786606-X-Ray Diffraction
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pubmed:year |
2002
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pubmed:articleTitle |
Chiral amplification of oligopeptides in two-dimensional crystalline self-assemblies on water.
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pubmed:affiliation |
Department of Materials and Interfaces, Weizmann Institute of Science, 76100 Rehovot, Israel.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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