▪ 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 …

In this review we bring together and discuss a number of different manifestations of a
chemicalsensing paradigm sometimes called the resistivepulse method. In the simplest …

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

To find motifs that mediate helix-helix interactions in membrane proteins, we have analyzed
frequently occurring combinations of residues in a database of transmembrane domains …

▪ Abstract Helical membrane protein folding and oligomerization can be usefully
conceptualized as involving two energetically distinct stages—the formation and subsequent …

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

One of the great challenges for molecular biologists is to learn how a protein sequence
defines its three-dimensional structure. For many years, the problem was even more difficult …

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 …

We have observed a common sequence motif in membrane proteins, which we call a
glycine zipper. Glycine zipper motifs are strongly overrepresented and conserved in …

Paramyxoviruses are responsible for significant human mortality and disease worldwide, but
the molecular mechanisms underlying their entry into host cells remain poorly understood …