59 research outputs found
Conformational studies of Zn-Ligand-Hexose diastereomers using ion mobility measurements and density functional theory calculations
Copper(II) complexes of oligopeptides:an equilibrium and spectroscopic study on the copper(II) lys-leu-ala-his-phe-gly system
CD spectroscopic study on the speciation and solution structure of copper(II) complexes of some tripeptides in combination with potentiometric and spectrophotometric results
Prospective and Daily Measures of Acute Thoughts, Decisional Struggle, and Coping: Measurement Correspondence and the Prediction of Exercise in Young Adults
S77C-ÎC7-CueR: a 199mHg PAC Study of the Protein Metal Site Structure
The CueR protein regulates the cytosolic concentration of Cu(I) in bacteria such as E. coli. With this work we aimed to remodel the linear two-coordinate metal site with Cys112 and Cys120 as ligands in CueR to a tricoordinate site similar to that observed in the Hg(II) sensor protein MerR. This was done by introducing an additional cysteine near the metal site in the modified S77C-ÎC7-CueR variant, inspired by the fact that Ser77 in CueR is replaced by a cysteine in MerR. 199m Hg PAC spectroscopic data indicate that two NQIs are present at pH 8.0, most likely reflecting HgS 2 and HgS 3 coordination modes, and demonstrating that the design of a pure HgS 3 metal site was not achieved. Lowering the pH to 6.0 or the temperature to â196 °C had surprisingly similar effects, giving rise to highly distorted trigonal Hg(II) coordination. Tentatively, this might reflect that the histidine just next to Cys77 (His76) coordinates forming a HgS 2 N metal site structure. Further redesign beyond the first coordination sphere appears to be required to efficiently stabilize the HgS 3 metal site structure at physiological pH
Is the Glass Half-Full or Half-Empty? The Relationship of Big and Little Optimism With Acute and Longer Term Exercise-Related Social Cognitions
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