Cooperativity between two transcription regulators occurs through protein-protein interactions with a general transcription factor complex and potentiates the parallel evolution of their DNA binding sites.
Hemoglobin affinity and cooperativity reveal mechanistic insights in how the relation between physiology and evolutionary variations shape a protein's molecular property.
Bacteria reach swimming speeds of several hundred body lengths per second and change direction in less than 5 ms by using coordinated flagella bundle agitation.
Metabolic switches between oxidative phosphorylation and aerobic glycolysis plus glutaminolysis direct T cell function by altering the flux of glucose and glutamine to N-glycosylation.
The sharp expression pattern driven by a classic, simple animal enhancer is determined by multiple molecular mechanisms, not only cooperative binding of the activating transcription factor as was previously thought.
A novel algorithm is used to solve the first 3D reconstruction of a stepping kinesin dimer on microtubules, directly visualizing the conformational effects of inter-head strain and giving novel insights into the motility mechanism.
A suppressor screen of dominant-negative synaptotagmin-induced lethality in Drosophila identifies key properties of the protein that regulate fusion, including the SNARE interaction surface.
A deep mutational coupling study demonstrates the ability of sequence coevolution methods to reveal the pattern of amino acid interactions underlying protein function.
A new analysis algorithm (DISC) enables accurate analysis of data from high-throughput single-molecule paradigms and reveals a non-cooperative binding mechanism of cyclic nucleotide-binding domains from HCN ion channels.
Regulation of the INO80 chromatin remodelling complex differs from those identified in other chromatin remodellers and involves a C-terminal domain of the Ino80 subunit.
