Trends in Biotechnology
ReviewElectrostatic interactions in aromatic oligopeptides contribute to protein stability
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Optimal Isotope Labeling of Aromatic Amino Acid Side Chains for NMR Studies of Protein Dynamics
2019, Methods in EnzymologyCitation Excerpt :Further, they are overrepresented in protein binding interfaces (Lo Conte, Chothia, & Janin, 1999), where they contribute a significant part of the binding free energy (Bogan & Thorn, 1998). Because of their quadrupolar electrostatic character, they can be engaged in specific interactions with other aromatic groups (Burley & Petsko, 1985, 1989), cations (Berry, Elvekrog, & Tommos, 2007; Mahadevi& Sastry, 2013), or sulfur (Valley et al., 2012). Tyr and especially His play an important role in enzyme activity (Bartlett, Porter, Borkakoti, & Thornton, 2002).
A mechanistic insight into protein-ligand interaction, folding, misfolding, aggregation and inhibition of protein aggregates: An overview
2018, International Journal of Biological MacromoleculesCitation Excerpt :Due to this reason plays an important role in protein-ligand interaction, folding etc. It is classified into three, dipole-dipole, charge-dipole, and charge–charge interaction [35]. The charge–charge interaction is applicable between the two oppositely charged species, ligand functional groups, or protein side chains, carboxyl group, phosphate groups, glutamate side chain are examples of negatively charged species while amine or imine groups, lysine, arginine, histidine are examples of positively charged species [36].
An Aromatic Cap Seals the Substrate Binding Site in an ECF-Type S Subunit for Riboflavin
2016, Journal of Molecular BiologyCitation Excerpt :In both structures, a conserved aromatic residue from Loop1-2 directly contacts the hydrophobic portion of the flavin ring. Specifically, both Phe33 of TmRibU and Tyr41 of SaRibU make an “edge-to-face” aromatic interaction [31] with the bound substrate (Fig. 3a). As a result, the conformation of Loop1-2, which undergoes a structural transition upon substrate binding [14,20], is largely conserved between the two structures.
The idiosyncrasies of tetrabenzo[24]crown-8 in the solid state
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