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Structural basis of PP2A activation by PTPA, an ATP-dependent activation chaperone
Proper activation of protein phosphatase 2A (PP2A) catalytic subunit is central for the complex PP2A regulation and is crucial for broad aspects of cellular function. The crystal structure of PP2AExpand
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Structural basis of protein phosphatase 2A stable latency
The catalytic subunit of protein phosphatase 2A (PP2Ac) is stabilized in a latent form by α4, a regulatory protein essential for cell survival and biogenesis of all PP2A complexes. Here we report theExpand
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Positioning the Intracellular Salt Potassium Glutamate in the Hofmeister Series by Chemical Unfolding Studies of NTL9.
In vitro, replacing KCl with potassium glutamate (KGlu), the Escherichia coli cytoplasmic salt and osmolyte, stabilizes folded proteins and protein-nucleic acid complexes. To understand the chemicalExpand
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Basis of Protein Stabilization by K Glutamate: Unfavorable Interactions with Carbon, Oxygen Groups.
Potassium glutamate (KGlu) is the primary Escherichia coli cytoplasmic salt. After sudden osmotic upshift, cytoplasmic KGlu concentration increases, initially because of water efflux and subsequentlyExpand
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The mechanism and high-free-energy transition state of lac repressor–lac operator interaction
Significant, otherwise-unavailable information about mechanisms and transition states (TS) of protein folding and binding is obtained from solute effects on rate constants. Here we characterize TSExpand
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Denaturant Probes Quantify the Preferential Burial of Amide Surface in Forming the Key Transition State and Early Intermediates in Protein Folding
Protein-folding has been extensively studied, but many questions remain regarding the mechanism. Characterizing early-unstable-intermediates and the high-free-energy transition-state (TS) will helpExpand