The placement of single methyl groups at certain positions in the sequence of small model transmembrane proteins consisting solely of leucines and isoleucines can modulate highly specific, productive interactions with the transmembrane domain of the erythropoietin receptor.
Weak yet highly species-specific protein-protein interactions enhance the activity of metabolically related enzymes in bacteria at endogenous conditions, but also mean that overexpression of one partner leads to permanent non-physiological complexes and gene dosage toxicity.
SPARK2 allows a transcriptional readout of inter- and intracellular protein-protein interactions, with near-zero background, by employing proximity-dependent luciferase-LOV regulation.
A biosensor resource has been developed to monitor the intracellular interactions of RAS family proteins with effector molecules and the effects of inhibitors as an aid to drug development.
A high-resolution method to quantify interactions between lipid bilayers and single proteins under controlled load is presented and applied to key proteins involved in membrane fusion and formation and maintenance of membrane contact sites.
Fluorescence detected sedimentation velocity offers a new method for studying heterogeneous protein interactions in solution by exploiting characteristic temporal signal modulations of photoswitchable fluorescent proteins.
A generalizable approach to understanding the logic of molecular recognition reveals the contributions of individual residues to the specificity of protein-protein interactions.
