Immunoglobulin‐type domains of titin are stabilized by amino‐terminal extension

FEBS Letters

Gautel, M¹  Pastore, A¹  Joseph, C¹  Politou, A.S¹ 

[1] European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany

关键词: Modular protein;    Muscle protein;    Boundary;    Protein stability;    Connectin;    CD;    circular dichroism;    ΔG;    Gibbs free energy change;    NMR;    nuclear magnetic resonance;    NTA;    nitrolotetra-acetic acid;    PCR;    polymerase chain reaction;    T m;    melting temperature UV;    ultraviolet;   

DOI  :  10.1016/0014-5793(94)00911-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown