Residue-specific information about the dynamics of antimicrobial peptides from (1)H-(15)N and (2)H solid-state NMR spectroscopy

Journal of the American Chemical Society
Kresten BertelsenThomas Vosegaard

Abstract

We present a new method to obtain information about the conformational dynamics of membrane-proteins using solid-state NMR experiments of oriented samples. By measuring the orientation-dependent (1)H-(15)N dipole-dipole coupling, (15)N anisotropic chemical shift, and (2)H quadrupole coupling parameters for a single residue, it is possible to obtain information about the local dynamics of each residue in the protein. This may be interpreted on an individual basis or through models extended to study conformational motion of membrane-protein segments. The method is demonstrated for the antimicrobial peptaibol alamethicin for which combined analysis of anisotropic interactions for the Aib(8) residue provides detailed information about helix-tilt angle, wobbling, and oscillatory rotation around the helix axis in the membrane bound state. This information is in very good agreement with coarse-grained MD simulations of the peptide in lipid bilayers.

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Citations

Oct 10, 2013·Protein & Cell·Conggang LiMaili Liu
Apr 18, 2014·The Journal of Physical Chemistry. B·Sara K HansenThomas Vosegaard
Mar 1, 2012·Chemistry and Physics of Lipids·Burkhard Bechinger, Evgeniy S Salnikov
Jul 19, 2013·Biochimica Et Biophysica Acta·Marco BortolusAnna Lisa Maniero
Aug 6, 2014·Journal of Magnetic Resonance·Zdeněk TošnerThomas Vosegaard
Jul 12, 2016·Solid State Nuclear Magnetic Resonance·Yusuke Nishiyama
Dec 31, 2019·Angewandte Chemie·Emmanuel O AwosanyaAlexander A Nevzorov
May 18, 2013·Chemistry & Biodiversity·László KredicsBalázs Leitgeb
Jun 9, 2012·The Journal of Physical Chemistry. B·Claudia U HjørringgaardTroels Skrydstrup
Apr 21, 2010·Biochimica Et Biophysica Acta·Maja Mihajlovic, Themis Lazaridis

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