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Title
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Immunoglobulin-type domains of titin are stabilized by amino-terminal extension.
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Authors
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A.S.Politou,
M.Gautel,
C.Joseph,
A.Pastore.
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Ref.
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FEBS Lett, 1994,
352,
27-31.
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PubMed id
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Abstract
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We have recently suggested that similarly folded titin modules located at
different sarcomeric regions have distinct molecular properties and stability.
Could our selection of module boundaries have potentially influenced our
conclusions? To address this question we expressed amino-terminally extended
versions of the same modules and determined, with the use of CD and Fluorescence
techniques, key thermodynamic parameters characterizing their stability. We
present here our results which confirm our previous observations and show that,
while amino-terminal extension has a profound effect on the stability of
individual modules, it does not affect at all their folding pattern or their
relative stabilities. Moreover, our data suggest that the selection of module
boundaries can be of critical importance for the structural analysis of modular
proteins in general, especially when a well-defined intron-exon topography is
absent and proteolytic methods are inconclusive.
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