Contributions of methionine to recognition of trimethyllysine in aromatic cage of PHD domains: implications of polarizability, hydrophobicity, and charge on binding
Katherine I. Albanese, Marcey L. Waters
Abstract
A conserved methionine in a trimethyllysine (Kme3) reader protein interacts <italic>via</italic> dispersion forces rather than ion-dipole interactions or the hydrophobic effect. Differences in selectivity for Kme3 <italic>versus</italic> its neutral analog were also discovered.
Topics & Concepts
PolarizabilityChemistryDipoleMethionineCharge (physics)CageChemical physicsCrystallographyBiophysicsBiochemistryMoleculeBiologyPhysicsOrganic chemistryAmino acidQuantum mechanicsCombinatoricsMathematicsMass Spectrometry Techniques and ApplicationsChemical Synthesis and AnalysisPolyamine Metabolism and Applications