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Using NMR spectroscopy and site-directed mutagenesis, we demonstrate that the Rad6b binding site, for the Rad18 RING domain, strongly resembles that of other E2/E3 RING/U-box complexes.
Utilizing confocal microscopy and site-directed mutagenesis, we demonstrate that three functional monopartite NLSs are located in a region of unknown function in the human MSH6 NTR.
In addition, using structure-based mutagenesis, we demonstrate that the putative interface region of TEM8 with PA (consisting of residues 56, 57, and 154 160) is responsible for the PA-binding affinity differences between the two receptors.
Using directed mutagenesis, we demonstrate that the amphipathic properties of Pex11-Amph are crucial for the function of Pex11 in peroxisome fission in vivo.
Using mutagenesis, we demonstrate that the nonselective filter from NsvBa can be converted into one that is more selective for Na+ or Ca2+, and that these features can be conferred onto the NaChBac filter.
We identified a similar conserved 1-8-14 1-8-14 1-8-14nding motif within the suppressor domain of IP3R1 and, using peptides and mutagenesis, we demonstrate that it is essential for IP3R activation, whether assessed by IP3-evoked Ca2+ release or patch-clamotifcoding of nuclear IP3R.
Similar(54)
Using homology-based structure modeling and site-directed mutagenesis, we demonstrated that one amino acid residue determines the different product specificity of PtTPS19 and PtTPS20.
Using mutagenesis experiments, we demonstrate that the mechanical stabilization effect is due to only a few key interactions of the protein with its ligand.
Using deletion mutagenesis, we also demonstrate the possible functional relevance of five of these genes.
In fact, by site directed mutagenesis, we could demonstrate the specificity of these boxes.
Using sequential deletion constructs of the three uATGs (ΔATG 1 3) generated by site-directed mutagenesis we could demonstrate that the translation effiency from the same construct was significantly increased when the uORFs were removed.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com