Operonic mRNAs in bacteria are comprised of ORF (open reading frame)-wide units of secondary structure, which are intrinsically distinct between adjacent ORFs and encode a rough blueprint for ORF-specific translation efficiency.
Multi-modal structural data fusion questions the specificity of fMRI-behavior associations by providing strong evidence relating human brain structure to a wide range of behavioral measures previously associated to functional connectivity.
Structural and biochemical studies indicate that AAA+ ATPase employ a general mechanism to translocate a variety of substrates, including extended polypeptides, hairpins, crosslinked chains, and chains conjugated to other molecules.
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.
Discovery of the structural basis for recognition and uptake of a human precursor for body odour production reveals an important role for bacterial peptide transport and novel routes to prevent its production in humans.
A domain-general structure learning mechanism, supported by anterior insula, moves beyond explicit category labels and dyadic similarity as the sole inputs to social group representations and predicts ally-choice behavior.
Distinct binding of viral proteins to the same region on the nucleosome surface can result in contrasting changes to higher-order chromatin structure in the host cell.
A structural and functional analysis of the electron transfer complex between a sulfite oxidase and its redox protein partner reveals an elegant compromise between the requirements for fast and efficient electron transfer and reaction specificity.
Structural analysis of the kinesin-13 MCAK bound to its C-terminal tail reveals the molecular basis for the conformation of kinesin-13 in solution and the mechanism that triggers long-range conformational changes upon microtubule binding.
Structures of a TMEM16 phospholipid scramblase reveal that its Ca2+-dependent activation entails global conformational changes and how these rearrangements affect the membrane to enable transbilayer lipid transfer.
