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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
35
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pubmed:dateCreated |
1994-1-13
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pubmed:abstractText |
Small angle x-ray scattering and viscometric analyses of the alpha-zeins of maize in solution indicated that the molecules were asymmetric. Structure predictions of consensus sequences for the two classes of alpha-zeins, Z19 and Z22, were in good agreement with the alpha-helical contents determined by circular dichroism. Dimensions determined by small angle x-ray scattering and viscometry indicated a predominantly alpha-helical conformation. The data are discussed in relation to models for the solution conformation and to earlier models for alpha-zeins structure.
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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 |
Dec
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
268
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
26253-9
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pubmed:dateRevised |
2002-11-1
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pubmed:meshHeading |
pubmed-meshheading:8253747-Amino Acid Sequence,
pubmed-meshheading:8253747-Circular Dichroism,
pubmed-meshheading:8253747-Molecular Sequence Data,
pubmed-meshheading:8253747-Protein Conformation,
pubmed-meshheading:8253747-Scattering, Radiation,
pubmed-meshheading:8253747-Solutions,
pubmed-meshheading:8253747-Zea mays,
pubmed-meshheading:8253747-Zein
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pubmed:year |
1993
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pubmed:articleTitle |
Solution conformational analysis of the alpha-zein proteins of maize.
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pubmed:affiliation |
Department of Agricultural Sciences, University of Bristol, United Kingdom.
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pubmed:publicationType |
Journal Article
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