HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article ACCEPTED PREPRINT Full Text (PDF) All Versions of this Article: ps.035840.108v1 17/8/1319    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Google Scholar Articles by Chugh, J. Articles by Hosur, R. PubMed PubMed Citation Articles by Chugh, J. Articles by Hosur, R. Social Bookmarking                   What's this?

Accelerated Communication

NMR insights into a Mega-Dalton size protein self-assembly

Tata Institute of Fundamental Research

(RECEIVED April 16, 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 mega-Dalton 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 which have remained difficult till date.

Keywords: Protein Structure/Folding; NMR Spectroscopy; Heteronuclear NMR; Relaxation measurements; Circular dichroism; Self-assembly

¹ E-mail: hosur{at}tifr.res.in

CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?