A schematic of the post-translational modifications of tubulin tails.

C-Terminal Tail Polyglycylation and Polyglutamylation Alter Microtubule Mechanical Properties

Oct. 14, 2022

We found that microtubule post-translational modifications affect bending rigidity.

Thumbnail image for Wall and Hough 2018 BiophysJ

In-Cell NMR within Budding Yeast Reveals Cytoplasmic Masking of Hydrophobic Residues of FG Repeats

April 19, 2019

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.

Thumbnail image for Wall et al. 2016 ACS Chem. Biol. paper

Molecular determinants of tubulin's C-terminal tail conformational ensemble

Aug. 19, 2016

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.

Kathryn Wall's paper accepted by ACS Chemical Biology

Aug. 16, 2016

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 .