Structural aspects of the solvation shell of lysine and acetylated lysine: A Car-Parrinello and classical molecular dynamics investigation

V. Carnevale, Simone Raugei

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Lysine acetylation is a post-translational modification, which modulates the affinity of protein-protein and/or protein-DNA complexes. Its crucial role as a switch in signaling pathways highlights the relevance of charged chemical groups in determining the interactions between water and biomolecules. A great effort has been recently devoted to assess the reliability of classical molecular dynamics simulations in describing the solvation properties of charged moieties. In the spirit of these investigations, we performed classical and Car-Parrinello molecular dynamics simulations on lysine and acetylated-lysine in aqueous solution. A comparative analysis between the two computational schemes is presented with a focus on the first solvation shell of the charged groups. An accurate structural analysis unveils subtle, yet statistically significant, differences which are discussed in connection to the significant electronic density charge transfer occurring between the solute and the surrounding water molecules.

Original languageEnglish
Article number225103
JournalJournal of Chemical Physics
Volume131
Issue number22
DOIs
Publication statusPublished - 2009

Fingerprint

lysine
Solvation
Molecular Dynamics Simulation
Lysine
solvation
Molecular dynamics
Railroad cars
molecular dynamics
proteins
acetylation
Acetylation
Proteins
Water
Computer simulation
Biomolecules
Post Translational Protein Processing
structural analysis
Structural analysis
water
affinity

ASJC Scopus subject areas

  • Physics and Astronomy(all)
  • Physical and Theoretical Chemistry
  • Medicine(all)

Cite this

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