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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1999-1-6
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pubmed:abstractText |
In situ Fourier transform infrared microspectroscopy was used to study the heat stability of proteins and hydrogen bonding interactions in dry maturation-defective mutant seeds of Arabidopsis thaliana. alpha-Helical, turn and beta-sheet conformations were the major protein secondary structures in all of these seeds. On heating, intermolecular extended beta-sheet structures, typical of protein denaturation, were formed in abscisic acid-insensitive (abi3) and leafy cotyledon (lec) mutant seeds. Proteins in dry wild-type seeds did not denature up to 150 degrees C, but those in dry desiccation-sensitive, lec1-1, lec1-3 and abi3-5 seeds did at 68, 89 and 87 degrees C, respectively. In the desiccation-tolerant abi3-7 and abi3-1 seeds, denaturation commenced above 120 and 135 degrees C, respectively. Seeds of the aba1-1 abi3-1 double mutant showed signs of denaturation already upon drying. The molecular packing in the seeds was studied by observing the shift in the position of the OH-stretching vibration band with temperature. The maximal rate of change of this band with temperature was much higher in the desiccation-sensitive abi3-5, aba1-1 abi3-1, lec1-1, and lec1-3 mutant seeds than in the desiccation-tolerant wild-type, abi3-1, abi3-7, and lec2-1 seeds. We interpret this to mean that the molecular packing density is higher in dry desiccation-tolerant than in dry desiccation-sensitive seeds, which is associated with a higher or lower protein denaturation temperature, respectively. The results are discussed in relation to the physiological and biochemical characteristics of these mutant seeds.
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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/ABI3 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carbohydrates,
http://linkedlifedata.com/resource/pubmed/chemical/Lipids,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0960-7412
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
133-43
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:9839460-Arabidopsis,
pubmed-meshheading:9839460-Arabidopsis Proteins,
pubmed-meshheading:9839460-Carbohydrates,
pubmed-meshheading:9839460-Genotype,
pubmed-meshheading:9839460-Hot Temperature,
pubmed-meshheading:9839460-Lipids,
pubmed-meshheading:9839460-Mutation,
pubmed-meshheading:9839460-Plant Proteins,
pubmed-meshheading:9839460-Protein Structure, Secondary,
pubmed-meshheading:9839460-Seeds,
pubmed-meshheading:9839460-Spectroscopy, Fourier Transform Infrared
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pubmed:year |
1998
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pubmed:articleTitle |
Properties of proteins and the glassy matrix in maturation-defective mutant seeds of Arabidopsis thaliana.
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pubmed:affiliation |
Department of Biomolecular Sciences, Wageningen Agricultural University, The Netherlands. Wim.Wolkers@algem.pf.wau.nl
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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