Immunoglobulin-type domains of titin are stabilized by amino-terminal extension (Journal article)

Politou, A. S./ Gautel, M./ Joseph, C./ Pastore, A.

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.
Institution and School/Department of submitter: Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής
Keywords: Amino Acid Sequence,Circular Dichroism,Conserved Sequence,Hydrogen-Ion Concentration,Immunoglobulins/chemistry,Molecular Sequence Data,Muscle Proteins/*chemistry,Oligopeptides/chemistry/*physiology,Protein Denaturation,*Protein Folding,*Protein Kinases,Protein Structure, Tertiary,Sequence Alignment,Thermodynamics
ISSN: 0014-5793
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

Files in This Item:
File Description SizeFormat 
Politou-1994-Immunoglobulin-type.pdf544.48 kBAdobe PDFView/Open    Request a copy

 Please use this identifier to cite or link to this item:
  This item is a favorite for 0 people.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.