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NMR insights into a megadalton-size protein self-assembly

Department of Chemical Sciences, Tata Institute of Fundamental Research, Mumbai 400005, India

(RECEIVED April 16, 2008; FINAL REVISION May 18, 2008; ACCEPTED May 20, 2008)

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.

Keywords: protein folding; self-assembly; Gdn-HCl; relaxation measurement; NMR

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