The number of contacts at the interface of a protein–protein complex, together with the properties of the surface, provides a simple, but well-performing predictor of binding affinity.
The range of molecular forms adopted by L1 retrotransposons reflect a tapestry of lifecycle-permissive and -restrictive host-parasite interactions occurring within cells.
The absolute affinities of thousands of variant antibodies are measured in parallel using a combination of cell sorting and high-throughput DNA sequencing.
Clustered and non-clustered protocadherins form antiparallel homodimers in which distinct regions of the extended interface demonstrate a division of labor between driving affinity and determining specificity.
ATP consumption enables chaperones to exploit the different kinetic properties of their conformational states to exhibit a non-equilibrium affinity for their substrates that is orders of magnitude higher than its equilibrium value.
Affinity capture of polyribosomes followed by RNAseq(ACAPSeq) is a technique that harnesses massively parallel sequencing to identify protein-protein interactions from any source from which polyribosomes can be purified.
High affinity interactions with transport adaptors are important to shield the interaction surfaces of cytomatrix components to block fatal premature oligomerization of active zone proteins during axonal transport.
The affinity of circadian repressors CRY1 and CRY2 for their cognate transcription factor CLOCK:BMAL1 is regulated by differential dynamics at the serine loop and interactions with the PER2 corepressor.
