The coiled coil is a common structural motif, formed by approximately 3±5% of all amino
acids in proteins.[1] Typically, it consists of two to five a-helices wrapped around each other …

Abstract α-Helical coiled coils are versatile protein domains, supporting a wide range of
biological functions. Their fold is probably better understood than that of any other protein; …

Protein design allows sequence-to-structure relationships in proteins to be examined and,
potentially, new protein structures and functions to be made to order. To succeed, however …

The nucleocapsid (N-) protein of severe acute respiratory syndrome coronavirus 2 (SARS-
CoV-2) has a key role in viral assembly and scaffolding of the viral RNA. It promotes liquid …

▪ Abstract The chemosensory pathway of bacterial chemotaxis has become a paradigm for
the two-component superfamily of receptor-regulated phosphorylation pathways. This …

▪ Abstract De novo protein design has recently emerged as an attractive approach for
studying the structure and function of proteins. This approach critically tests our …

Coiled-coil motifs provide simple systems for studying molecular self-assembly. We
designed two 28-residue peptides to assemble into an extended coiled-coil fiber …

In membrane proteins, the extent to which polarity, hydrogen bonding, and van der Waals
packing interactions of the buried, internal residues direct protein folding and association of …

The functional switch of glutamine/asparagine (Q/N)-rich prions and the neurotoxicity of
polyQ-expanded proteins involve complex aggregation-prone structural transitions …

Polar residues in transmembrane α-helices may strongly influence the folding or association
of integral membrane proteins. To test whether a motif that promotes helix association in a …