Water solubility and structural stability are key merits for proteins defined by the primary
sequence and 3D-conformation. Their manipulation represents important aspects of the …

Proteins are molecular machines whose function depends on their ability to achieve
complex folds with precisely defined structural and dynamic properties. The rational design …

The design of peptides that assemble in membranes to form functional ion channels is
challenging. Specifically, hydrophobic interactions must be designed between the peptides …

The computational design of transmembrane proteins with more than one membrane-
spanning region remains a major challenge. We report the design of transmembrane …

Transmembrane (TM) helices of integral membrane proteins can facilitate strong and
specific noncovalent protein–protein interactions. Mutagenesis and structural analyses have …

The features that stabilize the structures of membrane proteins remain poorly understood.
Polar interactions contribute modestly, and the hydrophobic effect contributes little to the …

Conspectus Transmembrane proteins located within biological membranes play a crucial
role in a variety of important cellular processes, such as energy conversion and signal …

The exquisite structure-function correlations observed in filamentous protein assemblies
provide a paradigm for the design of synthetic peptide-based nanomaterials. However, the …

Interaction between transmembrane helices often determines biological activity of
membrane proteins. Bitopic proteins, a broad subclass of membrane proteins, form dimers …

Single-pass membrane receptors contain extracellular domains that respond to external
stimuli and transmit information to intracellular domains through a single transmembrane …