NMR insights into a megadalton-size protein self-assembly

Chugh, Jeetender ; Sharma, Shilpy ; Hosur, Ramakrishna V. (2008) NMR insights into a megadalton-size protein self-assembly Protein Science, 17 (8). pp. 1319-1325. ISSN 0961-8368

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Official URL: http://onlinelibrary.wiley.com/doi/10.1110/ps.0358...

Related URL: http://dx.doi.org/10.1110/ps.035840.108


Protein self-association is critical to many biological functions. However, atomic-level structural characterization of these assemblies has remained elusive. In this report we present insights into the mechanistic details of the process of self-association of the 136-residue GTPase effector domain (GED) of the endocytic protein dynamin into a megadalton-sized soluble mass. Our approach is based on NMR monitoring of regulated folding and association through Gdn-HCl titration. The results suggest the evolution of a sequence-self-association paradigm. Equally significantly, the study demonstrates an elegant bottom-up strategy that can render large protein self-assemblies accessible to NMR investigations that have remained difficult to date.

Item Type:Article
Source:Copyright of this article belongs to Cold Spring Harbor Laboratory Press.
Keywords:Protein Folding; Self-assembly; Gdn-HCl; Relaxation Measurement; NMR
ID Code:16622
Deposited On:15 Nov 2010 13:33
Last Modified:17 May 2016 01:21

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