Antimicrobial peptides (AMPs) have remarkably different structures as well as biological
activity profiles, whereupon most of these peptides are supposed to kill bacteria via …

Concepts of solid-state NMR spectroscopy and applications to fluid membranes are
reviewed in this paper. Membrane lipids with 2H-labeled acyl chains or polar head groups …

Even 30 years after the discovery of magainins, biophysical and structural investigations on
how these peptides interact with membranes can still bear surprises and add new …

Solid-state NMR spectroscopy has much advanced during the last decade and provides a
multitude of data that can be used for high-resolution structure determination of …

Multicellular organisms fight bacterial and fungal infections by producing peptide-derived
broad-spectrum antibiotics. These host-defense peptides compromise the integrity of …

Solid-state NMR spectroscopic techniques provide valuable information about the structure,
dynamics and topology of membrane-inserted polypeptides. In particular antimicrobial …

The very amino-terminal domain of the huntingtin protein is directly located upstream of the
protein's polyglutamine tract, plays a decisive role in several important properties of this …

The interactions between peptides and lipids are of fundamental importance in the
functioning of numerous membrane-mediated cellular processes including antimicrobial …

Biophysical and structural studies of peptide–lipid interactions, peptide topology and
dynamics have changed our view on how antimicrobial peptides insert and interact with …

Various recent developments in solid-state nuclear magnetic resonance (ssNMR)
spectroscopy have enabled an array of new insights regarding the structure, dynamics, and …