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.
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.
An enrichable cross-linker with optional isotope labeling quadruples the number of cross-linked peptides identified from high-complexity samples, enhancing proteome-wide analysis of protein-protein interactions and protein conformational changes by mass spectrometry.