Adsorptive separation is very important in industry. Generally, the process uses porous solid materials such as zeolites, activated carbons, or silica gels as adsorbents. With an ever increasing need for a more efficient, energy-saving, and environmentally benign procedure for gas separation, adsorbents with tailored structures and tunable surface properties must be found. Metal–organic frameworks (MOFs), constructed by metal-containing nodes connected by organic bridges, are such a new type of porous materials. They are promising candidates as adsorbents for gas separations due to their large surface areas, adjustable pore sizes and controllable properties, as well as acceptable thermal stability. This critical review starts with a brief introduction to gas separation and purification based on selective adsorption, followed by a review of gas selective adsorption in rigid and flexible MOFs. Based on possible mechanisms, selective adsorptions observed in MOFs are classified, and primary relationships between adsorption properties and framework features are analyzed. As a specific example of tailor-made MOFs, mesh-adjustable molecular sieves are emphasized and the underlying working mechanism elucidated. In addition to the experimental aspect, theoretical investigations from adsorption equilibrium to diffusion dynamics via molecular simulations are also briefly reviewed. Furthermore, gas separations in MOFs, including the molecular sieving effect, kinetic separation, the quantum sieving effect for H2/D2 separation, and MOF-based membranes are also summarized (227 references).

Selective gas adsorption and separation in metal–organic frameworks

High performance liquid chromatographic determination of subpicomole amounts of amino acids by precolumn fluorescence derivatization with o-phthaldialdehyde

https://web.iitd.ac.in/~arunku/files/CEL311_Y13/Adsorption%20Theory%20to%20practice_Dabrowski.pdf

Adsorption — from theory to practice

Hydrophilic-interaction chromatography for the separation of peptides, nucleic acids and other polar compounds

The quantification of differences between two or more physiological states of a biological system is among the most important but also most challenging technical tasks in proteomics. In addition to the classical methods of differential protein gel or blot staining by dyes and fluorophores, mass-spectrometry-based quantification methods have gained increasing popularity over the past five years. Most of these methods employ differential stable isotope labeling to create a specific mass tag that can be recognized by a mass spectrometer and at the same time provide the basis for quantification. These mass tags can be introduced into proteins or peptides (i) metabolically, (ii) by chemical means, (iii) enzymatically, or (iv) provided by spiked synthetic peptide standards. In contrast, label-free quantification approaches aim to correlate the mass spectrometric signal of intact proteolytic peptides or the number of peptide sequencing events with the relative or absolute protein quantity directly. In this review, we critically examine the more commonly used quantitative mass spectrometry methods for their individual merits and discuss challenges in arriving at meaningful interpretations of quantitative proteomic data.

/pdf/quantitative-mass-spectrometry-in-proteomics-a-critical-510v02gycj.pdf

Quantitative mass spectrometry in proteomics: a critical review

Solvophobic interactions in liquid chromatography with nonpolar stationary phases

Salt effect on hydrophobic interactions in precipitation and chromatography of proteins: an interpretation of the lyotropic series.

The effect of solute ionization on the retention of weak acids, bases, and ampholytes on octadecylsilica was investigated both theoretically and experimentally. The retention was at­ tributed to a reversible association of the solutes with the hydrocarbonaceous ligand of the stationary phase. A phe­ nomenological treatment of the corresponding equilibria was developed for various types of ionogenic substances. The energetics of the association process was analyzed in a rig­ orous fashion in the light of the solvophobic theory and a semi-empirical extension of the Debye-Hiickel theory to high ionic strength. The predicted effect of solute ionization on the capacity factors was substantiated by experimental data. The observed dependence of the capacity factors on the ionic strength of the eluent and the hydrophobic surface of the solute molecules showed good agreement with the theory. The ad­ vantages of the technique in the separation of biological sub­ stances are illustrated.

Liquid chromatography of ionogenic substances with nonpolar stationary phases

Operating parameters and separation of nucleotides on pellicular ion exchangers investigated by liquid chromatographic system

Csaba Horváth

Papers

Solvophobic interactions in liquid chromatography with nonpolar stationary phases

Salt effect on hydrophobic interactions in precipitation and chromatography of proteins: an interpretation of the lyotropic series.

Liquid chromatography of ionogenic substances with nonpolar stationary phases

Fast liquid chromatography - An investigation of operating parameters and the separation of nucleotides on pellicular ion exchangers.

Capillary columns with in situ formed porous monolithic packing for micro high-performance liquid chromatography and capillary electrochromatography