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.

The core autophagy protein Atg8 plays non-autophagy roles through binding to an integral membrane protein Hfl1, which harbors an unusual Atg8-interacting motif.

The cotranslational membrane integration of three multispanning Escherichia coli inner membrane proteins is followed using force profile analysis, uncovering unexpected complexities in the membrane integration process.

An example of a deep learning-based strategy to discover novel protein-protein interactions and predict their complex structures at high accuracy.

Unbiased molecular dynamics simulations reveal the insertion mechanism of the lipidated tail of the matrix domain of HIV-1 Gag into realistic membrane models and show its effect on lipid sorting.

A hierarchical model explains the self-organization of membrane microdoomaims.

Atomistic simulations reveal how lipids can allosterically modulate membrane receptors.

The structure of a bivalent double-knot tarantula toxin bound to the outer pore of the capsaicin receptor reveals a novel mode of toxin-channel recognition that has important implications for thermosensation.

Computation and experiment together demonstrate that nonspecific membrane–protein interactions could regulate transmembrane protein function and suggest that covalent linkers can be an integral component of the sensing apparatus.

A single amino acid residue is critical for cardiolipin interaction specificity and nuclear membrane recruitment of a dynamin-related protein.