A comparison between the unfolding of fibronectin and contactin
| Autor: | Małgorzata Lekka, Janusz Lekki, A Dabrowska, Wojciech M. Kwiatek, K. Lebed |
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| Rok vydání: | 2006 |
| Předmět: | |
| Zdroj: | Journal of Physics: Condensed Matter. 18:10157-10164 |
| ISSN: | 1361-648X 0953-8984 |
| Popis: | The mechanical unfolding of two proteins belonging to the immunoglobulin superfamily, fibronectin (an extracellular matrix protein) and contactin (a neuronal adhesion protein), was studied by means of atomic force microscopy (AFM). The mean unfolding forces and characteristic lengths describing unfolding events of two types of the immunoglobulin module observed for contactin were compared with results obtained for fibronectin. The results showed that the FnIII-type domain present in both proteins, i.e. in contactin and fibronectin, requires a similar force of about 100 pN to be unfolded. However, the IgC2-type domains of contactin, normally remaining intact in view of the intra-domain disulfide bonds, reveal rather lower stability in the presence of the reducing agent. The force needed to unfold a single IgC2 domain was calculated and established to be about 70 pN. Initially, natural human fibronectin was chosen only as a reference protein for studies of contactin unfolding force values. However, interesting results were obtained and used as a reference in further analysis of the contactin unfolding pathway. Two characteristic length values were obtained for the FnIII domain type of both studied proteins; thus for both domains the ability to unravel in two different pathways was concluded. |
| Databáze: | OpenAIRE |
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