The biogenesis, folding, and structure of α-helical membrane proteins (MPs) are important to
understand because they underlie virtually all physiological processes in cells including key …

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

The intermolecular H‐bonding density heavily influences the gelation and rheological
behavior of hydrogen‐bonded supramolecular polymer hydrogels, thus offering a delicate …

▪ 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 …

Implicit solvent models for biomolecular simulations are reviewed and their underlying
statistical mechanical basis is discussed. The fundamental quantity that implicit models seek …

To execute their many vital functions, cell membranes are highly organized. Here, we review
how membrane structure shapes signal transduction across membranes. Recent …

The thermodynamic principles underlying the structural stability of membrane proteins are
difficult to obtain directly from whole proteins because of intractable problems related to …

Anionic, monolayer-protected gold nanoparticles (AuNPs) have been shown to
nondisruptively penetrate cellular membranes. Here, we show that a critical first step in the …

Introduction to Proteins provides a comprehensive and state-of-the-art introduction to the
structure, function, and motion of proteins for students, faculty, and researchers at all levels …

The first dynamical simulation of a protein based on a detailed atomic model was reported in
1977. Since then, the uses of various theoretical and computational approaches have …