DNA motifs tuned for low affinity binding of BMP-induced pMad/Medea transcription factors function to restrict gene activation to small subsets of the many Drosophila neurons that exhibit active BMP signaling.
Detailed and inferred model reproduces B-cell affinity distributions measured in mice immunized according to various protocols and explains non-monotonous effects of antigen dosage on maturation.
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.
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.
