Lipid Dynamics Studied by Calculation of 31P Solid-State NMR Spectra Using Ensembles from Molecular Dynamics Simulations

TY - JOUR

T1 - Lipid Dynamics Studied by Calculation of 31P Solid-State NMR Spectra Using Ensembles from Molecular Dynamics Simulations

AU - Hansen, Sara Krogh

AU - Vestergaard, Mikkel

AU - Thøgersen, Lea

AU - Schiøtt, Birgit

AU - Nielsen, Niels Christian

AU - Vosegaard, Thomas

PY - 2014

Y1 - 2014

N2 - We present a method to calculate 31P solid-state NMR spectra based on the dynamic input from extended molecular dynamics (MD) simulations. The dynamic information confered by MD simulations is much more comprehensive than the information provided by traditional NMR dynamics models based on, for example, order parameters. Therefore, valuable insight into the dynamics of biomolecules may be achieved by the present method. We have applied this method to study the dynamics of lipid bilayers containing the antimicrobial peptide alamethicin, and we show that the calculated 31P spectra obtained with input from MD simulations are in agreement with experiments under a large range of different sample conditions, including vesicles and oriented samples with and without peptides. We find that the changes in the 31P spectra upon addition of peptide stem from lipids with reduced diffusion due to peptide–lipid interactions.

AB - We present a method to calculate 31P solid-state NMR spectra based on the dynamic input from extended molecular dynamics (MD) simulations. The dynamic information confered by MD simulations is much more comprehensive than the information provided by traditional NMR dynamics models based on, for example, order parameters. Therefore, valuable insight into the dynamics of biomolecules may be achieved by the present method. We have applied this method to study the dynamics of lipid bilayers containing the antimicrobial peptide alamethicin, and we show that the calculated 31P spectra obtained with input from MD simulations are in agreement with experiments under a large range of different sample conditions, including vesicles and oriented samples with and without peptides. We find that the changes in the 31P spectra upon addition of peptide stem from lipids with reduced diffusion due to peptide–lipid interactions.

U2 - 10.1021/jp5000304

DO - 10.1021/jp5000304

M3 - Journal article

C2 - 24738559

SN - 1520-6106

VL - 118

SP - 5119

EP - 5129

JO - Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical

JF - Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical

IS - 19

ER -