Charged and polar groups, through forming ion pairs, hydrogen bonds, and other less
specific electrostatic interactions, impart important properties to proteins. Modulation of the …

The structure and function of biomolecules are strongly influenced by their hydration shells.
Structural fluctuations and molecular excitations of hydrating water molecules cover a broad …

Despite the great importance of membrane proteins, structural and functional studies of
these proteins present major challenges. A significant hurdle is the extraction of the …

Advances over the past 25 years have revealed much about how the structural properties of
membranes and associated proteins are linked to the thermodynamics and kinetics of …

Membrane permeabilizing peptides (MPPs) are as ubiquitous as the lipid bilayer
membranes they act upon. Produced by all forms of life, most membrane permeabilizing …

Antimicrobial peptides (AMPs) have been studied for three decades, and yet a molecular
understanding of their mechanism of action is still lacking. Here we summarize current …

The partitioning of membrane-active oligopeptides into membrane interfaces promotes the
formation of secondary structure. A quantitative description of the coupling of structure …

▪ Abstract Stably folded membrane proteins reside in a free energy minimum determined by
the interactions of the peptide chains with each other, the lipid bilayer hydrocarbon core, the …

A new simulation method, dissipative particle dynamics, is applied to model biological
membranes. In this method, several atoms are united into a single simulation particle. The …

The lipid bilayer component of biological membranes is important for the distribution,
organization, and function of bilayer-spanning proteins. This regulation is due to both …