1H, 15N, 13C resonance assignment of 9.7 M urea-denatured state of the GTPase effector domain (GED) of dynamin

Chugh, Jeetender ; Sharma, Shilpy ; Kumar, Dinesh ; Hosur, Ramakrishna V. (2009) 1H, 15N, 13C resonance assignment of 9.7 M urea-denatured state of the GTPase effector domain (GED) of dynamin Biomolecular NMR Assignments, 3 (1). pp. 13-16. ISSN 1874-2718

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Official URL: http://www.springerlink.com/content/5ql064n28v1430...

Related URL: http://dx.doi.org/10.1007/s12104-008-9129-1

Abstract

The GTPase effector domain (GED) of dynamin, a multi-domain protein involved in endocytosis, forms a megadalton-sized self-assembly (even at micromolar concentrations) in native conditions in vitro. While such large assemblies have remained inaccessible to detailed NMR structural characterization, till date, a significant recent achievement has been the elucidation of the GED association pathway starting from a Gdn-HCl denatured monomer. Since, the nature of the denaturant has a strong influence on the conformational preferences in the denatured states, and hence on the association pathways, or even on the final assembly, we report here the NMR resonance assignment of 9.7 M urea-denatured GED from Homo sapiens. This will form the basis for the characterization of the association pathways and the final assembly driven by urea dilution.

Item Type:Article
Source:Copyright of this article belongs to Springer-Verlag.
Keywords:GTPase Effector Domain; NMR; Resonance Assignment; Self-assembly; Urea-denatured State
ID Code:16621
Deposited On:15 Nov 2010 13:33
Last Modified:03 Jun 2011 08:38

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