The brain obtains and preserves a consistent temporal alignment of multisensory and motor information flowing along staggered streams by maintaining an invariant estimate across modalities of the energy exchanged with the environment at discrete events.

Single-molecule force and fluorescence spectroscopy reveal the structural states and dynamics of E. coli single-stranded DNA binding proteins and the energy landscape of the nucleo–protein complex.

Cellular immunity against Toxoplasma parasites is orchestrated by GBP complexes attacking the parasite membrane.

A novel strategy is presented for quantitatively measuring protein-DNA and protein-protein interactions that regulate transcription in living cells.

Integration of structural bioinformatics and free-energy simulations reveals how a helicase switches its function from unwinding to rezipping DNA, during which a key metastable conformation is predicted and verified by single-molecule measurements.

Rigorous reanalysis of single-molecule data yields evidence for energy expenditure in the interaction of transcription factors on DNA.

Mapping the locations of hypertrophic cardiomyopathy gene variants onto the three-dimensional structures of contractile proteins revealed that these disrupt protein interactions are critical for normal cardiac relaxation and efficient energy usage.

Interactions between HIV-1 Env and human mannose receptor enhance HIV entry but restrict viral egress and spread in the absence of Vpr.

An interaction between the brown fat protein CIDEA and the phospholipid phosphatidic acid is vital for the expansion of intracellular lipid droplets for energy storage.

Fluorescence resonance energy transfer has been used to explore the interactions between DNA polymerases, sliding clamps and clamp loaders as DNA is replicated in human cells.