Karlsruhe Institute of Technology-ko ikertzaileekin lankidetzan egindako argitalpenak (8)

2014

  1. 19F NMR screening of unrelated antimicrobial peptides shows that membrane interactions are largely governed by lipids

    Biochimica et Biophysica Acta - Biomembranes, Vol. 1838, Núm. 9, pp. 2260-2268

2013

  1. Canonical azimuthal rotations and flanking residues constrain the orientation of transmembrane helices

    Biophysical Journal, Vol. 104, Núm. 7, pp. 1508-1516

2012

  1. Comparative analysis of the orientation of transmembrane peptides using solid-state 2H- and 15N-NMR: Mobility matters

    European Biophysics Journal, Vol. 41, Núm. 5, pp. 475-482

  2. Hydrophobic mismatch of mobile transmembrane helices: Merging theory and experiments

    Biochimica et Biophysica Acta - Biomembranes, Vol. 1818, Núm. 5, pp. 1242-1249

2010

  1. Solid state NMR analysis of peptides in membranes: Influence of dynamics and labeling scheme

    Biochimica et Biophysica Acta - Biomembranes, Vol. 1798, Núm. 2, pp. 252-257

2009

  1. Influence of whole-body dynamics on 15N PISEMA NMR spectra of membrane proteins: A theoretical analysis

    Biophysical Journal, Vol. 96, Núm. 8, pp. 3233-3241

  2. Orientation and dynamics of peptides in membranes calculated from 2H-NMR data

    Biophysical Journal, Vol. 96, Núm. 8, pp. 3223-3232

2008

  1. Solid state NMR structure analysis of the antimicrobial peptide gramicidin s in lipid membranes: Concentration-dependent re-alignment and self-assembly as a β-barrel

    Topics in Current Chemistry, Vol. 273, pp. 139-154