Methyl-Induced Polarization Destabilizes the Noncovalent Interactions of N-Methylated Lysines.

ABSTRACT: Lysine methylation can modify noncovalent interactions by altering lysine's hydrophobicity as well as its electronic structure. Although the ramifications of the former are documented, the effects of the latter remain largely unknown. Understanding the electronic structure is important for determining how biological methylation modulates protein-protein binding, and the impact of artificial methylation experiments in which methylated lysines are used as spectroscopic probes and protein crystallization facilitators. The benchmarked first-principles calculations undertaken here reveal that methyl-induced polarization weakens the electrostatic attraction of amines with protein functional groups - salt bridges, hydrogen bonds and cation-π interactions weaken by as much as 10.3, 7.9 and 3.5 kT,

SUBMITTER: Rahman S 

PROVIDER: S-EPMC9830558 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature