108 research outputs found
Design and Estimation for Domains
Peer Reviewedhttps://deepblue.lib.umich.edu/bitstream/2027.42/147156/1/rssd00081.pd
Optima and Proxima in Linear Sample Designs
Peer Reviewedhttps://deepblue.lib.umich.edu/bitstream/2027.42/147006/1/rssa04086.pd
Optima and Proxima in Linear Sample Designs
Peer Reviewedhttps://deepblue.lib.umich.edu/bitstream/2027.42/147135/1/rssa03594.pd
Inference from Complex Samples
Peer Reviewedhttps://deepblue.lib.umich.edu/bitstream/2027.42/146969/1/rssb00981.pd
Book reviews
Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/45702/1/11336_2005_Article_BF02289852.pd
Lactose intolerance among severely malnourished children with diarrhoea admitted to the nutrition unit, Mulago hospital, Uganda
The dynamic stator stalk of rotary ATPases
Rotary ATPases couple ATP hydrolysis/synthesis with proton translocation across biological membranes and so are central components of the biological energy conversion machinery. Their peripheral stalks are essential components that counteract torque generated by rotation of the central stalk during ATP synthesis or hydrolysis. Here we present a 2.25-Ă… resolution crystal structure of the peripheral stalk from Thermus thermophilus A-type ATPase/synthase. We identify bending and twisting motions inherent within the structure that accommodate and complement a radial wobbling of the ATPase headgroup as it progresses through its catalytic cycles, while still retaining azimuthal stiffness necessary to counteract rotation of the central stalk. The conformational freedom of the peripheral stalk is dictated by its unusual right-handed coiled-coil architecture, which is in principle conserved across all rotary ATPases. In context of the intact enzyme, the dynamics of the peripheral stalks provides a potential mechanism for cooperativity between distant parts of rotary ATPases
On The Differentiation Of Ecological Units.
PhDSociologyUniversity of Michigan, Horace H. Rackham School of Graduate Studieshttp://deepblue.lib.umich.edu/bitstream/2027.42/183355/2/0003777.pd
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