E
Erik Strandberg
Researcher at Karlsruhe Institute of Technology
Publications - 64
Citations - 2630
Erik Strandberg is an academic researcher from Karlsruhe Institute of Technology. The author has contributed to research in topics: Lipid bilayer & Antimicrobial peptides. The author has an hindex of 28, co-authored 58 publications receiving 2327 citations.
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Journal ArticleDOI
Tilt Angles of Transmembrane Model Peptides in Oriented and Non-Oriented Lipid Bilayers as Determined by 2H Solid-State NMR
Erik Strandberg,Suat Özdirekcan,Dirk T. S. Rijkers,Patrick C.A. van der Wel,Roger E. Koeppe,Rob M. J. Liskamp,J. Antoinette Killian +6 more
TL;DR: These properties allow application of the GALA method not only to macroscopically aligned samples but also to randomly oriented samples, which has important practical advantages, and is shown to be energetically unfavorable.
Journal ArticleDOI
NMR methods for studying membrane‐active antimicrobial peptides
Erik Strandberg,Anne S. Ulrich +1 more
TL;DR: Different approaches are outlined here, with an emphasis on solid state NMR methods, to study the structures of antimicrobial peptides in lipid bilayers as well as the effect of these peptides on model membranes.
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Concentration-Dependent Realignment of the Antimicrobial Peptide PGLa in Lipid Membranes Observed by Solid-State 19F-NMR
Ralf W. Glaser,Carsten Sachse,Ulrich H.N. Dürr,Parvesh Wadhwani,Sergii Afonin,Erik Strandberg,Anne S. Ulrich +6 more
TL;DR: The membrane-disruptive antimicrobial peptide PGLa is found to change its orientation in a dimyristoyl-phosphatidylcholine bilayer when its concentration is increased to biologically active levels.
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2H-NMR study and molecular dynamics simulation of the location, alignment, and mobility of pyrene in POPC bilayers.
TL;DR: It is seen that pyrene prefers a position inside the lipid membrane near the headgroups and has no tendency to diffuse from one monolayer of the membrane to the other, and the normal of the molecular plane is aligned nearly perpendicular to the bilayer normal.
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Conformation and Membrane Orientation of Amphiphilic Helical Peptides by Oriented Circular Dichroism
Jochen Bürck,Siegmar Roth,Parvesh Wadhwani,Sergii Afonin,Nathalie Kanithasen,Erik Strandberg,Anne S. Ulrich +6 more
TL;DR: Changes in peptide conformation and membrane alignment observed here by OCD seem to be functionally relevant, as they can be correlated with the membrane perturbing activities of the three antimicrobial and cell-penetrating sequences.