Preparation of heterogeneous TiO2/g-C3N4 with a layered mosaic stack structure by use of montmorillonite as a hard template approach: TC degradation, kinetic, mechanism, pathway and DFT investigation

: In the present study, SAPO-34 particles were synthesized using hydrothermal (HT) and dry gel (DG) conversion methods in the presence of diethyl amine (DEA) as an organic structure directing agent (SDA). Carbon nanotubes (CNT) were used as hard template in the synthesis procedure to introduce transport pores into the structures of the synthesized samples. The synthesized samples were characterized with different methods to reveal effects of synthesis method and using hard template on their structure and catalytic performance in methanol to olefin reaction (MTO). DG conversion method results in smaller particle size in comparison with hydrothermal method, resulting in enhancing catalytic performance. On the other side, using CNT in the synthesis procedure with DG method results in more reduction in particle size and formation of hierarchical structure which drastically improves catalytic performance.

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Degradation Kinetic and Pharmacokinetic Studies of Quercetin Chitosan Nanoparticles Using Validated Ultra High Performance Liquid Chromatography- Synapt Mass Spectrometry (UPLC-MS/MS-ESI-Q-TOF)

Current Pharmaceutical Analysis ◽

10.2174/1573412913666170503121839 ◽

2018 ◽

Vol 14 (3) ◽

pp. 286-297 ◽

Cited By ~ 1

Author(s):

Niyaz Ahmad ◽

Rizwan Ahmad ◽

Atta Abbas Naqvi ◽

Md Aftab Alam ◽

Rehan Abdur Rub ◽

...

Keyword(s):

Mass Spectrometry ◽

High Performance Liquid Chromatography ◽

Liquid Chromatography ◽

High Performance ◽

Chitosan Nanoparticles ◽

Pharmacokinetic Studies ◽

Degradation Kinetic

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Simulation studies of the interactions between membrane proteins and detergents

Biochemical Society Transactions ◽

10.1042/bst0330910 ◽

2005 ◽

Vol 33 (5) ◽

pp. 910-912 ◽

Cited By ~ 6

Author(s):

P.J. Bond ◽

J. Cuthbertson ◽

M.S.P. Sansom

Keyword(s):

Membrane Proteins ◽

Membrane Protein ◽

Self Assembly ◽

Kinetic Mechanism ◽

Coarse Grained ◽

Simulation Studies ◽

High Resolution Data ◽

Biologically Relevant ◽

Structure And Dynamics ◽

Detergent Interactions

Interactions between membrane proteins and detergents are important in biophysical and structural studies and are also biologically relevant in the context of folding and transport. Despite a paucity of high-resolution data on protein–detergent interactions, novel methods and increased computational power enable simulations to provide a means of understanding such interactions in detail. Simulations have been used to compare the effect of lipid or detergent on the structure and dynamics of membrane proteins. Moreover, some of the longest and most complex simulations to date have been used to observe the spontaneous formation of membrane protein–detergent micelles. Common mechanistic steps in the micelle self-assembly process were identified for both α-helical and β-barrel membrane proteins, and a simple kinetic mechanism was proposed. Recently, simplified (i.e. coarse-grained) models have been utilized to follow long timescale transitions in membrane protein–detergent assemblies.

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