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Full-Text Articles in Physical Sciences and Mathematics
Room Temperature Ionic Liquid Templated Meso-Macroporous Material By Self-Assembled Giant Gold Nanoparticles And Its Enhancement On The Direct Electrochemistry Of Cytochrome C, Pei Li, Dong-Ping Zhan, Yuan-Hua Shao
Room Temperature Ionic Liquid Templated Meso-Macroporous Material By Self-Assembled Giant Gold Nanoparticles And Its Enhancement On The Direct Electrochemistry Of Cytochrome C, Pei Li, Dong-Ping Zhan, Yuan-Hua Shao
Journal of Electrochemistry
Room temperature ionic liquid (RTIL) is used as a soft-template to organize a meso-macroporous material constructed by self-assembled giant gold nanoparticles which are capped by L-cysteine. First, L-cysteine capped gold nanoparticles can self-assembly to form nanowires and sub-micrometer spherical giant particles due to the static interaction and/or the condensation reaction between the carboxyl and amino groups at the outer terminal of the ligand. Second, the spherical assembled particles can form a quasi-solid gel when grinding with a hydrophobic RTIL, 1-octyl-3-metyllimidazolium hexafluorophosphate. Finally, when the composite gel is coated on a glassy carbon electrode and then polarized by using cyclic voltammetry …
Protein Conformational Studies By Hydrogen/Deuterium Exchange Mass Spectrometry, Antony D. Rodriguez
Protein Conformational Studies By Hydrogen/Deuterium Exchange Mass Spectrometry, Antony D. Rodriguez
Electronic Thesis and Dissertation Repository
Proteins are biological macromolecules responsible for the majority of all physiological processes. In order to properly function proteins are required to adopt highly ordered structures. These structural aspects may be found within a single protein or arise from multi-protein complexes. Here hydrogen/deuterium exchange mass spectrometry (HDX-MS) is employed as a tool to determine the extent of protein higher order structure. Exposure to D2O-based solvent causes the heavier isotope to exchange with amide hydrogens in the polypeptide backbone. This exchange is mainly dependent on protein conformation because the presence of stable hydrogen-bonded secondary structure will impede the incorporation of …