We have performed a structure-function analysis of actin by mutating residues involved in nucleotide hydrolysis and assaying the effects of these mutations on actin assembly in vitro and in vivo.
To understand the biological effects of these mutations, his team has genetically modified a mouse in the same way as the people who stutter.
The effects of these mutations were tested using neuropeptide Y receptors Y1R and Y2R.
The next phase of research will focus on studying the biologic effects of these mutations and how they give rise to seizures.
For six most frequently occurring mutations, the corresponding single mutants were created to dissect the effects of these mutations.
In parallel, we measure the effects of these mutations on the free energy of assembling the homotetrameric transmembrane pore from monomeric helices in micelles and bilayers.
The structure was used to engineer surface mutations in Rap1, and the effects of these mutations on silencing and telomere length regulation were assayed in vivo.
The effects of these mutations were examined by monitoring expression of a firefly luciferase (luc) reporter gene under the control of NahR.
Furthermore, we carried out docking simulation studies that could partially explain the effects of these mutations on C3′-specific hydroxylation activity.
To investigate a structural hypothesis for the effects of these mutations, we performed homology modeling of the pore region of wild-type and mutant KCNQ3 channels, using KvAP as a template.
In addition, the synergistic effects of these mutations on organic solvent tolerance were ambiguous.
