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M Dathe

Showing results (21-30 of 33) with videos related to

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FEBS Letters|December 12, 1997
Modulation of membrane activity of amphipathic, antibacterial peptides by slight modifications of the hydrophobic momentT Wieprecht, M Dathe, E Krause, et al.
International Journal of Peptide and Protein Research|May 1, 1996
Conformational differences of ovine and human corticotropin releasing hormone. A CD, IR, NMR and dynamic light scattering studyM Dathe, H Fabian, K Gast, et al.
Biochemistry|May 20, 1997
Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranesT Wieprecht, M Dathe, M Beyermann, et al.
Journal of Peptide Science : an Official Publication of the European Peptide Society|May 14, 1999
Structural requirements for cellular uptake of alpha-helical amphipathic peptidesA Scheller, J Oehlke, B Wiesner, et al.
The British Journal of Dermatology|September 14, 2020
Development of a pathogenesis-based therapy for peeling skin syndrome type 1F Valentin, H Wiegmann, T Tarinski, et al.
European Journal of Pharmacology|November 30, 1995
Influence of alpha-helicity, amphipathicity and D-amino acid incorporation on the peptide-induced mast cell activationL J Cross, M Ennis, E Krause, et al.
The Journal of Biological Chemistry|February 22, 2000
A role for a helical connector between two receptor binding sites of a long-chain peptide hormoneM Beyermann, S Rothemund, N Heinrich, et al.
Biochemistry|September 24, 1996
Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranesM Dathe, M Schümann, T Wieprecht, et al.
FEBS Letters|February 17, 1997
Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptidesM Dathe, T Wieprecht, H Nikolenko, et al.
Biochemistry|October 23, 1997
Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antibacterial peptidesT Wieprecht, M Dathe, R M Epand, et al.
Pageof 4

Showing results (21-30 of 33) with videos related to

Sort By:
Pageof 4
FEBS Letters|December 12, 1997
Modulation of membrane activity of amphipathic, antibacterial peptides by slight modifications of the hydrophobic momentT Wieprecht, M Dathe, E Krause, et al.
International Journal of Peptide and Protein Research|May 1, 1996
Conformational differences of ovine and human corticotropin releasing hormone. A CD, IR, NMR and dynamic light scattering studyM Dathe, H Fabian, K Gast, et al.
Biochemistry|May 20, 1997
Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranesT Wieprecht, M Dathe, M Beyermann, et al.
Journal of Peptide Science : an Official Publication of the European Peptide Society|May 14, 1999
Structural requirements for cellular uptake of alpha-helical amphipathic peptidesA Scheller, J Oehlke, B Wiesner, et al.
The British Journal of Dermatology|September 14, 2020
Development of a pathogenesis-based therapy for peeling skin syndrome type 1F Valentin, H Wiegmann, T Tarinski, et al.
European Journal of Pharmacology|November 30, 1995
Influence of alpha-helicity, amphipathicity and D-amino acid incorporation on the peptide-induced mast cell activationL J Cross, M Ennis, E Krause, et al.
The Journal of Biological Chemistry|February 22, 2000
A role for a helical connector between two receptor binding sites of a long-chain peptide hormoneM Beyermann, S Rothemund, N Heinrich, et al.
Biochemistry|September 24, 1996
Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranesM Dathe, M Schümann, T Wieprecht, et al.
FEBS Letters|February 17, 1997
Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptidesM Dathe, T Wieprecht, H Nikolenko, et al.
Biochemistry|October 23, 1997
Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antibacterial peptidesT Wieprecht, M Dathe, R M Epand, et al.
Pageof 4