Browse our latest Biochemistry and Chemical Biology articles

The centromeric protein CENP-T assembles the microtubule-binding interface of kinetochores through direct recruitment of two Ndc80 complexes and indirect recruitment of a third one through the Mis12 complex.

The hepatitis C virus IRES binds and remodels preassembled eukaryotic translation preinitiation complexes, using specific initiation factor protein within a "bacterial-like" mode of initiation that can function in both stressed and unstressed cells.

Oriented hexasomes can be generated using the Widom 601 positioning sequence, which enables straightforward production of nucleosomes with asymmetrically modified H2A/H2B dimers.

Biochemical and structural analyses of a universal mRNP remodeling pathway suggest an ATPase-powered targeted deposition of export factors onto mRNP.

Biochemical dissections show that the Guided Entry of Tail Anchored proteins (GET) pathway selects ER-destined tail-anchored proteins using at least two distinct molecular mechanisms, each recognizing a distinct physicochemical feature in the substrate.

Meiotic cells employ a specific pathway to limit the amount of gene conversion occuring at recombination sites.

Cyanine fluorophores are encoded as non-canonical amino acids to produce functional proteins in cell-free translation systems and live cells for single-molecule imaging.

Diverse biophysical properties of β1 and β3 integrin transmembrane and cytoplasmic domains result in distinct mechanisms of integrin activation and function.

Atomic structures of hIAPP fibrillar segments, determined using the cryo electron microscopy method MicroED, reveal that strong, stable intermolecular interactions are important features of cytotoxic amyloid proteins.

Evolutionary bioinformatics and experimentation are applied to the components of the Tat protein transport system to elucidate the structure of the membrane-bound receptor complex and to deduce a molecular description for its substrate-triggered activation.