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To address this question we expressed amino\u2010terminally 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\u2010terminal 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\u2010defined intron\u2014exon topography is absent and proteolytic methods are inconclusive.<\/jats:p>","DOI":"10.1016\/0014-5793(94)00911-2","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T09:39:31Z","timestamp":1027589971000},"page":"27-31","source":"Crossref","is-referenced-by-count":46,"title":["Immunoglobulin\u2010type domains of titin are stabilized by amino\u2010terminal 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