Rhomboids are intramembrane serine proteases that cleave the transmembrane helices of
substrate proteins, typically releasing luminal/extracellular domains from the membrane …

The cleavage of protein inside cell membranes regulates pathological pathways and is a
subject of major interest. Thus, the nature of the coupling between the physical environment …

The majority of oligomeric proteins form clusters which have rotational or dihedral symmetry.
Despite the many advantages of symmetric packing, protein oligomers are only nearly …

Intramembrane proteases hydrolyze peptide bonds within the membrane as a regulatory
paradigm that is conserved across all forms of cellular life. Many of these enzymes are …

Rhomboids comprise a broad family of intramembrane serine proteases that are found in a
wide range of organisms and participate in a diverse array of biological processes. High …

Many c-type cytochromes (cyts) can form domain-swapped oligomers. The positively
charged Hydrogenobacter thermophilus (HT) cytochrome (cyt) c 552 forms domain-swapped …

Chemical shift assignments of large membrane proteins by solid-state NMR experiments are
challenging. Recent advancements in sensitivity-enhanced pulse sequences, have made it …

The rhomboid family of intramembrane serine proteases are capable of cleaving
transmembrane protein substrates embedded within the phospholipid membrane. This …

Rhomboids are intramembrane serine proteases that cleave transmembrane (TM) protein
substrates within the phospholipid bilayer. Since the discovery of the first rhomboid …

Membrane proteins are a diverse range of macromolecules and when misfolded, disease
phenotypes often occur. Membrane protein folding studies ascertain how a linear …