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Disc electrophoresis.
Solution NMR Studies of the Aβ(1−40) and Aβ(1−42) Peptides Establish that the Met35 Oxidation State Affects the Mechanism of Amyloid Formation
With the use of a special disaggregation protocol, the highly aggregation prone Aβ peptides could be studied at higher, millimolar concentrations (as required by NMR) in aqueous solution at neutral pH, remaining largely monomeric at 5 °C as determined by the NMR results.
Solution NMR studies of the A beta(1-40) and A beta(1-42) peptides establish that the Met35 oxidation state affects the mechanism of amyloid formation.
The present NMR studies demonstrate that the Met35(red) --> Met 35(ox) conversion prevents aggregation by reducing both hydrophobic and electrostatic association and that the highly aggregation prone A beta peptides may associate differently, through specific, sharp changes in structure during the initial stages of aggregation.
A conserved region in the σ54‐dependent activator DctD is involved in both binding to RNA polymerase and coupling ATP hydrolysis to activation
Data suggest that the N‐terminal half of the C3 region of DctD contains a site that may contact σ54‐holoenzyme during open complex formation.
Mechanism of enolase: the crystal structure of asymmetric dimer enolase-2-phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0 A resolution.
The crystal structure of a complex between yeast enolase and an equilibrium mixture of PGA and PEP is reported, indicating that the water molecule hydrating carbon-3 of PEP in the PEP --> PGA reaction is activated by the carboxylates of Glu168 and Glu211.
The structure of yeast enolase at 2.25-A resolution. An 8-fold beta + alpha-barrel with a novel beta beta alpha alpha (beta alpha)6 topology.
The three-dimensional structure of yeast enolase has been determined by the multiple isomorphous replacement method followed by the solvent flattening technique, and it supports the hypothesis that some enzymes evolved independently producing the stable structure of beta alpha barrels with either enol enzyme or triose phosphate isomerase topology.
Purification and properties of the heme- and iron-sulfur-containing heterodisulfide reductase from Methanosarcina thermophila.
Kinetic studies in which CO oxidation is coupled to heterodisulfide reduction strongly indicate that a membrane-associated compound is the direct electron donor to HDR and an electron-transfer pathway is presented that postulates a mechanism for coupling electron transport to proton translocation.
Yeast enolase: mechanism of activation by metal ions.
  • J. Brewer
  • Biology, Chemistry
    CRC critical reviews in biochemistry
  • 1981
There is an absolute correlation between the occurrence of a structural change undergone by the 3-amino analogue of phosphoenolpyruvate and whether the metal ions produce any level of enzymatic activity.
Interactions between immunoglobulin-like and catalytic modules in Clostridium thermocellum cellulosomal cellobiohydrolase CbhA.
The results indicate that inactivation of the GH9 module occurs as a result of multiple structural disturbances finally affecting the topology of the catalytic center.