Nanomechanical unfolding of α-neurexin: A major component of the synaptic junction

Autor:	Karolina Mikulska, Wieslaw Nowak, Aleksander Balter, J. Strzelecki
Rok vydání:	2012
Předmět:	Synapse Crystallography Molecular recognition Component (thermodynamics) Chemistry Atomic force microscopy Neurexin Force spectroscopy Biophysics General Physics and Astronomy Synaptic junction Physical and Theoretical Chemistry
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:	https://explore.openaire.eu/search/publication?articleId=doi_________::12b2379efc28ba57524b26c211c9a4b0 https://doi.org/10.1016/j.cplett.2011.11.033 Zobrazit plný text záznamu Full Text from ScienceDirect