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Structural Characterization of the Loop at the Alpha-Subunit C-Terminus of the Mixed Lineage Leukemia Protein Activating Protease Taspase1
A helix-turn-helix motif is proposed, which can be exploited as novel anticancer target to inhibit Taspase1 proteolytic activity and explored in six members of the type 2 asparaginase family using homology modeling.
Click Chemistry on the Surface of Ultrasmall Gold Nanoparticles (2 nm) for Covalent Ligand Attachment Followed by NMR Spectroscopy.
The uptake of these nanoparticles after 24 h by HeLa cells was very efficient and showed that the nanoparticles even penetrated the nuclear membrane to a very high degree (in contrast to dissolved FAM-alkyne alone that did not enter the cell).
Solution NMR Spectroscopy with Isotope-Labeled Cysteine (13C and 15N) Reveals the Surface Structure of l-Cysteine-Coated Ultrasmall Gold Nanoparticles (1.8 nm).
The surface structure and the coordination environment of the cysteine ligands on the ultrasmall gold nanoparticles were studied by a variety of homo- and heteronuclear NMR spectroscopic techniques, supported by geometric considerations of the nanoparticle ultrastructure.
DNA Mismatch‐Specific Base Flipping by a Bisacridine Macrocycle
The macrocyclic bisacridine BisA is demonstrated to be able to specifically recognize DNA base mismatches and most likely induces base flipping, which does not appear to be limited to DNA‐modifying enzymes but it is likely to also be induced by a small synthetic molecule binding to a thermodynamically weakened site in DNA.
An NMR Method To Pinpoint Supramolecular Ligand Binding to Basic Residues on Proteins.
The H2(C)N spectra track the terminal CH2 groups of all Lys and Arg residues, revealing significant differences in their binding kinetics and chemical shift perturbation, and can be used to clearly pinpoint the order of ligand binding.
Peptide-Conjugated Ultrasmall Gold Nanoparticles (2 nm) for Selective Protein Targeting
Ultrasmall gold nanoparticles with a metallic core diameter of 2 nm were surface-conjugated with peptides that selectively target epitopes on the surface of the WW domain of the model protein hPin1...
Specific inhibition of the Survivin–CRM1 interaction by peptide-modified molecular tweezers
A sophisticated strategy is reported addressing Survivin’s nuclear export signal (NES), the binding site of CRM1, with advanced supramolecular tweezers for lysine and arginine, to address a previously unapproachable protein surface area.