Biomolecular NMR Assignments

, Volume 5, Issue 1, pp 59–61 | Cite as

Resonance assignments of GTPase effector domain of dynamin in the aprotic solvent deuterated dimethyl sulfoxide

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Abstract

The GTPase effector domain (GED) is a subunit of dynamin, a multi-domain protein involved in endocytosis. GED forms a megadalton-sized self-assembly in vitro. The core of such huge assemblies is inaccessible to detailed Nuclear Magnetic Resonance characterization by conventional methods due to line broadening effects. Till date, there have been no studies to directly identify the residues involved in the core of the assembly. In this background we report here the NMR resonance assignments of deuterated dimethyl sulfoxide (DMSO-d6)-denatured GED from Homo sapiens. This will form the basis for probing the core of GED assembly and characterization of the association pathway driven by DMSO dilution.

Keywords

Assembly Deuterated dimethyl sulfoxide GTPase effector domain Nuclear magnetic resonance 
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Notes

Acknowledgments

We thank the Government of India for providing financial support to the National Facility for High Field NMR at TIFR and Dr. Rohit Mittal for the GED clone. The author acknowledges PM Krishnamohan for his help with the experiments and Manoj Kumar Rout for the help provided for learning CARA.

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Copyright information

© Springer Science+Business Media B.V. 2010

Authors and Affiliations

  1. 1.Department of Chemical SciencesTata Institute of Fundamental ResearchMumbaiIndia
  2. 2.UM-DAE Centre for Excellence in Basic SciencesSanta Cruz, MumbaiIndia

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