Insights into protein aggregation by NMR characterization of insoluble SH3 mutants solubilized in salt-free water.

ABSTRACT: Protein aggregation in vivo has been extensively associated with a large spectrum of human diseases. On the other hand, mechanistic insights into protein aggregation in vitro were incomplete due to the inability in solubilizing insoluble proteins for high-resolution biophysical investigations. However, a new avenue may be opened up by our recent discovery that previously-thought insoluble proteins can in fact be solubilized in salt-free water. Here we use this approach to study the NMR structural and dynamic properties of an insoluble SH3 mutant with a naturally-occurring insertion of Val22 at the tip of the diverging turn. The obtained results reveal: 1) regardless of whether the residue is Val, Ala, Asp or Arg, the insertion will render the first hNck2 SH3 domain to be insoluble in buffe

SUBMITTER: Liu J 

PROVIDER: S-EPMC2776303 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature