Tryptophan (Trp) holds a unique place in biology for a multitude of reasons. It is the largest
of all twenty amino acids in the translational toolbox. Its side chain is indole, which is …

β-Barrel outer membrane proteins (OMPs) represent the major proteinaceous component of
the outer membrane (OM) of Gram-negative bacteria. These proteins perform key roles in …

Antimicrobial peptides serve as a first line of innate immune defense against invading
organisms such as bacteria and viruses. In this study, we hypothesized that peptides …

The transfer free energies of the twenty natural amino acid side chains from water to
phospholipid bilayers make a major contribution to the assembly and function of membrane …

Tryptophan (Trp) is abundant in membrane proteins, preferentially residing near the lipid–
water interface where it is thought to play a significant anchoring role. Using a total of 3μs of …

Thermodynamic stabilities are pivotal for understanding structure–function relationships of
proteins, and yet such determinations are rare for membrane proteins. Moreover, the few …

In cells, β-barrel membrane proteins are transported in unfolded form to an outer membrane
into which they fold and insert. Model systems have been established to investigate the …

The biogenesis of transmembrane β-barrels (outer membrane proteins, or OMPs) is an
elaborate multistep orchestration of the nascent polypeptide with translocases, barrel …

Aromatic amino acids of membrane proteins are enriched at the lipid-water interface. The
role of tryptophan on the folding and stability of an integral membrane protein is investigated …

Accurate measurements of the thermodynamic stability of folded membrane proteins require
methods for monitoring their conformation that are free of experimental artifacts. For …