ArticleBiophysical journal2009
Influence of whole-body dynamics on 15N PISEMA NMR spectra of membrane proteins: a theoretical analysis.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 40 citations in OpenAlex.
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- A theoretical assessment of structure determination of multi-span membrane proteins by oriented sample solid-state NMR spectroscopy.Australian journal of chemistry · 2020Article
- NMR Structural Studies of Antimicrobial Peptides: LPcin Analogs.Biophysical journal · 2016Article
- 3D hydrophobic moment vectors as a tool to characterize the surface polarity of amphiphilic peptides.Biophysical journal · 2014Article
- Probing the transmembrane structure and dynamics of microsomal NADPH-cytochrome P450 oxidoreductase by solid-state NMR.Biophysical journal · 2014Article
- Comparison between the behavior of different hydrophobic peptides allowing membrane anchoring of proteins.Advances in colloid and interface science · 2014Review
- High-resolution structures and orientations of antimicrobial peptides piscidin 1 and piscidin 3 in fluid bilayers reveal tilting, kinking, and bilayer immersion.Journal of the American Chemical Society · 2014Article
- Supramolecular structure of membrane-associated polypeptides by combining solid-state NMR and molecular dynamics simulations.Biophysical journal · 2012Article
- Comparative analysis of the orientation of transmembrane peptides using solid-state (2)H- and (15)N-NMR: mobility matters.European biophysics journal : EBJ · 2012Article
- On the combined analysis of ²H and ¹⁵N/¹H solid-state NMR data for determination of transmembrane peptide orientation and dynamics.Biophysical journal · 2011Article
- Transmembrane helix orientation and dynamics: insights from ensemble dynamics with solid-state NMR observables.Biophysical journal · 2011Article
- A kinked antimicrobial peptide from Bombina maxima. II. Behavior in phospholipid bilayers.European biophysics journal : EBJ · 2011Article
- Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations.European biophysics journal : EBJ · 2011Article
- Charged or aromatic anchor residue dependence of transmembrane peptide tilt.The Journal of biological chemistry · 2010Article
- Interpretation of 2H-NMR experiments on the orientation of the transmembrane helix WALP23 by computer simulations.Biophysical journal · 2010Article
- Chemical shift tensor - the heart of NMR: Insights into biological aspects of proteins.Progress in nuclear magnetic resonance spectroscopy · 2010Review
- Proton-evolved local-field solid-state NMR studies of cytochrome b5 embedded in bicelles, revealing both structural and dynamical information.Journal of the American Chemical Society · 2010Article
- Orientation and dynamics of transmembrane peptides: the power of simple models.European biophysics journal : EBJ · 2010Review
- Tilt and rotation angles of a transmembrane model peptide as studied by fluorescence spectroscopy.Biophysical journal · 2009Article
- Orientation and dynamics of peptides in membranes calculated from 2H-NMR data.Biophysical journal · 2009Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane proteins and peptides exhibit a preferred orientation in the lipid bilayer while fluctuating in an anisotropic manner. Both the orientation and the dynamics have direct functional implications, but motions are usually not accessible, and structural descriptions are generally static. Using simulated data, we analyze systematically the impact of whole-body motions on the peptide orientations calculated from two-dimensional polarization inversion spin exchange at the magic angle (PISEMA) NMR. Fluctuations are found to have a significant effect on the observed spectra. Nevertheless, wheel-like patterns are still preserved, and it is possible to determine the average peptide tilt and azimuthal rotation angles using simple static models for the spectral fitting. For helical peptides undergoing large-amplitude fluctuations, as in the case of transmembrane monomers, improved fits can be achieved using an explicit dynamics model that includes Gaussian distributions of the orientational parameters. This method allows extracting the amplitudes of fluctuations of the tilt and azimuthal rotation angles. The analysis is further demonstrated by generating first a virtual PISEMA spectrum from a molecular dynamics trajectory of the model peptide, WLP23, in a lipid membrane. That way, the dynamics of the system from which the input spectrum originates is completely known at atomic detail and can thus be directly compared with the dynamic output obtained from the fit. We find that fitting our dynamics model to the polar index slant angles wheel gives an accurate description of the amplitude of underlying motions, together with the average peptide orientation.
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