Autor: |
Karolina Mikulska, Wieslaw Nowak, Aleksander Balter, J. Strzelecki |
Rok vydání: |
2012 |
Předmět: |
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Zdroj: |
Chemical Physics Letters. 521:134-137 |
ISSN: |
0009-2614 |
Popis: |
Neurexins are proteins involved in synapse signaling. Understanding molecular recognition in neurons requires a knowledge of neurexin elasticity at a single molecule level. We apply, for the first time, AFM force spectroscopy to reveal mechanical properties of rat neurexin 1α (NRXN1α). Spectra indicate a flexible hinge. The first event in the unfolding pathway is a change of neurexin shape accompanied by EGF-like E3 domain unfolding. This requires low forces on the order of 50 pN. The other LNS/LG domains require forces of 100 pN to be unfolded. The unfolding of core modules (L1–E1–L2) and (L3–E2–L4) is a two stage process. |
Databáze: |
OpenAIRE |
Externí odkaz: |
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