Outer membrane proteins (OMPs) play a central role in the integrity of the outer membrane
of Gram-negative bacteria. Unfolded OMPs (uOMPs) transit across the periplasm, and …

Just 25years ago the Anfinsen thermodynamic hypothesis was shown to be valid for
membrane proteins. Despite the complex biological machinery required for their in vivo …

The objective is to provide guidance for pregnant women and obstetric care and exercise
professionals on prenatal physical activity. The outcomes evaluated were maternal, fetal or …

Fundamental to the central goals of structural biology is knowledge of the energetics of
molecular interactions. Because membrane proteins reside in a free energy minimum …

The transfer free energies of the twenty natural amino acid side chains from water to
phospholipid bilayers make a major contribution to the assembly and function of membrane …

Here we describe how the systematic redesign of a protein's hydrophobic core alters its
structure and stability. We have repacked the hydrophobic core of the four‐helix‐bundle …

Little is known about the dynamic process of membrane protein folding, and few models
exist to explore it. In this study we doubled the number of Escherichia coli outer membrane …

Glycophorin A forms homodimers through interaction of the single, helical transmembrane
domains of the monomers. The dimers are stable in sodium dodecylsulfate (SDS), permitting …

Outer membrane β-barrel proteins (OMPs) are crucial for numerous cellular processes in
prokaryotes and eukaryotes. Despite extensive studies on OMP biogenesis, it is unclear why …

The outer membrane of Gram-negative bacteria is a unique asymmetric lipid bilayer
composed of phospholipids (PLs) in the inner leaflet and lipopolysaccharides (LPSs) in the …