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 Citations (Scopus)

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
Externally publishedYes

Fingerprint

Hydrogen bonds
hydrogen bonds
water
molecules
biopolymer denaturation
Molecules
Water
voids
simulation
interactions
molecular dynamics
proteins
Denaturation
N-methylacetamide
causes
hydrogen
Molecular dynamics
Proteins
Association reactions
Computer simulation

Keywords

  • MD simulation

ASJC Scopus subject areas

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

Cite this

Effect of pressure on the solution structure and hydrogen bond properties of aqueous N-methylacetamide. / Sarma, Rahul; Paul, Sandip.

In: Chemical Physics, Vol. 407, 15.10.2012, p. 115-123.

Research output: Contribution to journalArticle

@article{cb66559dec0d412496f2a70874ef8a7b,
title = "Effect of pressure on the solution structure and hydrogen bond properties of aqueous N-methylacetamide",
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.",
keywords = "MD simulation",
author = "Rahul Sarma and Sandip Paul",
year = "2012",
month = "10",
day = "15",
doi = "10.1016/j.chemphys.2012.09.014",
language = "English (US)",
volume = "407",
pages = "115--123",
journal = "Chemical Physics",
issn = "0301-0104",
publisher = "Elsevier",

}

TY - JOUR

T1 - Effect of pressure on the solution structure and hydrogen bond properties of aqueous N-methylacetamide

AU - Sarma, Rahul

AU - Paul, Sandip

PY - 2012/10/15

Y1 - 2012/10/15

N2 - 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.

AB - 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.

KW - MD simulation

UR - http://www.scopus.com/inward/record.url?scp=84868205097&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84868205097&partnerID=8YFLogxK

U2 - 10.1016/j.chemphys.2012.09.014

DO - 10.1016/j.chemphys.2012.09.014

M3 - Article

AN - SCOPUS:84868205097

VL - 407

SP - 115

EP - 123

JO - Chemical Physics

JF - Chemical Physics

SN - 0301-0104

ER -