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 majority of therapeutics target membrane proteins, accessible on the surface of cells, to
alter cellular signaling. Cells use membrane proteins to transduce signals into cells …

In order to identify strong transmembrane helix packing motifs, we have selected
transmembrane domains exhibiting high-affinity homo-oligomerization from a randomized …

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 …

Introduction Class I cytokines regulate key processes such as growth, lactation,
hematopoiesis, and immune function and contribute to oncogenesis. Although the …

Erythropoietin receptor (EPOR) is thought to be activated by ligand-induced
homodimerization. However, structures of agonist and antagonist peptide complexes of …

Helical integral membrane proteins share several structural determinants that are widely
conserved across their universe. The discovery of common motifs has furthered our …

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

The noncovalent association of transmembrane α-helices is a fundamental event in the
folding of helical membrane proteins. In this work, a system (TOXCAT) is developed for the …

Processing of the amyloid precursor protein (APP) by β‐and γ‐secretases leads to the
generation of amyloid‐β (Aβ) peptides with varying lengths. Particularly Aβ42 contributes to …