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Cover Image
Cover Image
Cover picture: Structural model of the membrane motor of the ATP synthase, inhibited by oligomycin. The model integrates cryo-EM and x-ray crystallography data with biochemical, functional, and evolutionary information. The model explains how the direction of rotation of the c-ring (marine) against subunit a (orange) is coupled to the direction of proton permeation and why oligomycin (yellow) blocks this mechanism in either direction. Positions where mutation confers resistance to oligomycin are marked with green and cyan spheres; blue and red spheres indicate some of the key residues for proton transport (see Research Article by Leone and Faraldo-Gómez, 441–457).
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Article
Structure and mechanism of the ATP synthase membrane motor inferred from quantitative integrative modeling
The ATP synthase is a molecular rotor that recycles ADP into ATP. Leone and Faraldo-Gómez use structural modeling to reinterpret and reconcile recent cryo-EM data for its membrane domain with other experimental evidence, gaining insights into its mechanism and the mode of inhibition by oligomycin.
Three-dimensional stochastic model of actin–myosin binding in the sarcomere lattice
Models of cellular contraction, for example, in striated muscle, usually involve mass action kinetics. Mijailovich et al. implement spatially explicit actomyosin interactions in the Monte Carlo platform MUSICO and show the extent to which myosin tethering affects other biological parameters.
Spatial model of convective solute transport in brain extracellular space does not support a “glymphatic” mechanism
A “glymphatic mechanism” has been proposed to mediate convective fluid transport from para-arterial to paravenous extracellular space in the brain. Jin et al. model such a system and find that diffusion, rather than convection, can account for the transport of solutes.
