Effect of pressure on the solution structure and hydrogen bond properties of aqueous N-methylacetamide

Rahul Sarma, Sandip Paul

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

Effects of high pressure on hydrophobic and hydrogen bonding interactions are investigated by employing molecular dynamics (MD) simulations of aqueous N-methylacetamide (NMA) solutions. Such systems are of interest mainly because high pressure causes protein denaturation and NMA is a computationally effective model to understand the atomic-level picture of pressure-induced structural transitions of protein. Simulations are performed for five different pressure values ranging from 1 atm to 8000 atm. We find that NMA molecules are associated mostly through their hydrophobic methyl groups and high pressure reduces this association propensity, causing dispersion of these moieties. At high pressure, structural void decreases and the packing efficiency of water molecules around NMA molecules increases. Hydrogen bond properties calculations show favorable NMA-NMA hydrogen bonds as compared to those of NMA-water hydrogen bonds and preference of NMA to be a hydrogen bond acceptor rather than a donor in interaction with water.

Original languageEnglish (US)
Pages (from-to)115-123
Number of pages9
JournalChemical Physics
Volume407
DOIs
StatePublished - Oct 15 2012

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Keywords

  • MD simulation

ASJC Scopus subject areas

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

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