10 research outputs found
Biomolecular Recognition of Methylated Histones
Lysine and arginine methylations are among the most abundant posttranslational modifications found on histone proteins. The recognition of methylated lysine and arginine residues by epigenetic reader proteins provides an important molecular requirement for regulation of human genes. Recent structural and mechanistic studies importantly advanced our basic understanding of biomolecular recognition of methylated histones by diverse classes of epigenetic readers. In this chapter, we describe chemical biological studies on the recognition of methylated histones by the aromatic cage-containing reader proteins.</p
Molecular-scale Hydrophilicity Induced by Solute: Molecular-thick Charged Pancakes of Aqueous Salt Solution on Hydrophobic Carbon-based Surfaces
Ion Enrichment on the Hydrophobic Carbon-based Surface in Aqueous Salt Solutions due to Cation-π Interactions
Selective binding of choline by a phosphate-coordination-based triple helicate featuring an aromatic box
The response of Ω-loop D dynamics to truncation of trimethyllysine 72 of yeast iso-1-cytochrome c depends on the nature of loop deformation
Exploiting non-covalent π interactions for catalyst design
Molecular recognition, binding and catalysis are often mediated by non-covalent interactions involving aromatic functional groups. Although the relative complexity of these so-called π interactions has made them challenging to study, theory and modelling have now reached the stage at which we can explain their physical origins and obtain reliable insight into their effects on molecular binding and chemical transformations. This offers opportunities for the rational manipulation of these complex non-covalent interactions and their direct incorporation into the design of small-molecule catalysts and enzymes
