In-cell NMR in S. cerevisiae is a novel way of looking at disordered proteins in a crowded cellular environment. The methodology has been developed here, which could be broadly applicable to other protein systems. In an example, the non-specific interactions of the FG Nup construct, FSFG-K, with the cytoplasm is similar to previously found bacterial interactions using NMR relaxation techniques. This work was recently published in Biophysical Journal.
The disordered C-terminal tails of tubulin are biologically important but difficult to study. We describe a method to isotopically label tubulin for structural studies by NMR of the C-terminal tails.
The paper "Molecular determinants of tubulin’s C-terminal tail conformational ensemble" by Kathryn Wall, Maria Pagratis, Geoffrey Armstrong, Jeremy Balsbaugh, Eric Verbeke, Chad Pearson, and Loren Hough was accepted to ACS Chemical Biology .
