Source:http://linkedlifedata.com/resource/pubmed/id/19137619
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2009-5-27
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pubmed:abstractText |
Tear lipocalin and beta-lactoglobulin are members of the lipocalin superfamily. They have similar tertiary structures but unusually low overall sequence similarity. Non-native helical structures are formed during the early stage of beta-lactoglobulin folding. To address whether the non-native helix formation is found in the folding of other lipocalin superfamily proteins, the folding kinetics of a tear lipocalin variant were investigated by stopped-flow methods measuring the time-dependent changes in circular dichroism (CD) spectrum and small-angle X-ray scattering (SAXS). CD spectrum showed that extensive secondary structures are not formed during a burst-phase (within a measurement dead time). The SAXS data showed that the radius of gyration becomes much smaller than in the unfolded state during the burst-phase, indicating that the molecule is collapsed during an early stage of folding. Therefore, non-native helix formation is not general for folding of all lipocalin family members. The non-native helix content in the burst-phase folding appears to depend on helical propensities of the amino acid sequence.
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pubmed:commentsCorrections | |
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 |
Jul
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pubmed:issn |
1097-0134
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pubmed:author |
pubmed-author:FujiwaraKazuoK,
pubmed-author:IkeguchiMasamichiM,
pubmed-author:KiharaHiroshiH,
pubmed-author:KuwajimaKunihiroK,
pubmed-author:MakiKosukeK,
pubmed-author:MatsumuraYoshitakaY,
pubmed-author:TsugeHideakiH,
pubmed-author:TsukamotoSeiichiS,
pubmed-author:YamadaYoshiteruY,
pubmed-author:YamashitaTakakoT
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pubmed:issnType |
Electronic
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pubmed:volume |
76
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
226-36
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pubmed:dateRevised |
2010-1-4
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pubmed:meshHeading |
pubmed-meshheading:19137619-Amino Acid Sequence,
pubmed-meshheading:19137619-Circular Dichroism,
pubmed-meshheading:19137619-Escherichia coli,
pubmed-meshheading:19137619-Humans,
pubmed-meshheading:19137619-Kinetics,
pubmed-meshheading:19137619-Lactoglobulins,
pubmed-meshheading:19137619-Lipocalin 1,
pubmed-meshheading:19137619-Molecular Sequence Data,
pubmed-meshheading:19137619-Point Mutation,
pubmed-meshheading:19137619-Protein Denaturation,
pubmed-meshheading:19137619-Protein Folding,
pubmed-meshheading:19137619-Protein Structure, Secondary,
pubmed-meshheading:19137619-Scattering, Small Angle,
pubmed-meshheading:19137619-Sequence Alignment,
pubmed-meshheading:19137619-Urea,
pubmed-meshheading:19137619-X-Ray Diffraction
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pubmed:year |
2009
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pubmed:articleTitle |
Non-native alpha-helix formation is not necessary for folding of lipocalin: comparison of burst-phase folding between tear lipocalin and beta-lactoglobulin.
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pubmed:affiliation |
Department of Bioinformatics, Soka University, Hachioji, Tokyo 192-8577, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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