Browse the search results

A giant multifunctional protein complex mediates mating-type recognition through a non-ligand–receptor mechanism in a multisexual species.

Chemical modifications near the tRNA anticodon and specific mRNA–tRNA pairs combine to control the ribosomal three-nucleotide mRNA reading frame, essential for the sequential addition of amino acids into polypeptide chains.

Molecular structure of mitochondrial complex I from Drosophila melanogaster reveals a structural element not seen in other organisms to date that may regulate the transition between an off-pathway resting state and the active state of the complex.

A new structure reveals two Arf-GEF regulatory domains form a single structural unit that stimulates Arf-GEF activity.

Components of the nuclear pore complex share structural and functional features with soluble nuclear transport receptors, which suggests that there may be an evolutionary relationship between these two types of protein.

It is technically difficult to identify transport proteins, but here a method is presented that exploits the principle that they are stabilized in detergent solution when they bind their substrate.

Stochastic mRNA and non-coding RNA hybridisation has a major impact on protein expression.

Construction of a first atomic model for an intact bacterial ATP synthase allows for a structural understanding of the roles of individual amino acids in the mechanism of ATP synthesis.

The structure of the entire Mot1 Swi2/Snf2 protein uncovers an unexpected auto-inhibited resting state activated by substrate binding, and suggests a DNA pulling mechanism of TBP displacement.

Noncanonical usage of stop codons in ciliates expands structurally flexible Q-rich domains and coevolves with codon usage biases to avoid triplet repeat disorders mediated by CAG/GTC replication slippage.