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Mass Spectrometry & Purification Techniques is an open access journal and the main aim of this journal to provide a platform for scientists, researchers in industry and academia all over the world to present their new ideas, discuss new strategies, and promote developments in all areas of Mass Spectrometry & Purification Techniques. Articles from all fields of scientific research in which purification techniques and mass spectrometry can play a key role will be considered. The fields include chemistry, physics, geology, environmental science, biological, health and life sciences. It is a scholarly Open Access journal and aims to publish the reliable source of information on the advanced research topics in the field of mass spectrometry & purification techniques.
The journal is intended to be comprehensive, and its main aim is to publish papers on both fundamentals and applications of mass spectrometry include instrumentation principles, design, and demonstration, chemical kinetics, mechanisms of ionization, theory of ion fragmentation, cluster ions, potential energy surfaces, and modeling, studies of thermodynamic properties, ion spectroscopy, structures and chemical properties of gas-phase ions. Mass Spectrometry application subjects include structural elucidation, biopolymer sequencing, development or validation of new methodology, proteomics, environmental and forensic measurements. Purification topics as chromatographic separation, protein purification, antibody purification, antigen fractionation, affinity purification, Liquid–Liquid extraction, adsorption, filtration, centrifugation, evaporation, crystallization, recrystallization, bioleaching protein purification, smelting, refining, distillation, water purification, electrolysis and downstream processing.
Mass Spectrometry & Purification Techniques journal is a scholarly Open Access journal maintains high standards of scientific excellence and its editorial board promises a rapid peer review process with the help of the Editorial Manager System. Manuscripts are accepted for publication only if at least two reviewers agree on the scientific quality of the manuscript.
Mass Spectrometry & Purification Techniques Journals are at higher echelons that enhance the intelligence and information dissemination on topics closely related to mass spectrometry and purification techniques. The Journal provides a unique forum dedicated to scientists to express their research articles, review articles, case reports and short communications on an array of mass spectrometry and purification research. Mass Spectrometry & Purification Techniques Peer Reviewed Journal is proficiently supported by universally prominent Editorial Board members. Abstracts and full texts of all articles published by the journal Mass Spectrometry & Purification Techniques or methods are freely accessible to everyone immediately after publication.
Mass spectrometry is an analytical technique that helps in identifying the quanity and type of chemical substances present in a sample by measuring the mass-to-charge ratio and abundance of gas-phase ions. The main components of mass spectrometry includes ion Source, mass analyser and detector. Principles of mass spectrometry includes qualitative and quantitative analysis providing information about the mass of atoms and molecules, molecular structure determination of organic & inorganic, identification and characterization of materials, creating gas phase ions from the analyte atoms or molecules, separating the ions according to their mass-to-charge ratio and measuring the abundance of the ions.
Related journals of Mass spectrometry
Journal of Chromatography & Separation Techniques, Journal of Environmental Analytical Chemistry, Journal of Environmental Analytical Chemistry, International Journal of Mass Spectrometry, Journal of The American Society for Mass Spectrometry, European Journal of Mass Spectrometry
Tandem mass spectrometery is a specialized instrument that detects molecules by measuring their weight. Tandem mass spectrometers measure weight electronically and display results in the form of a mass spectrum. A mass spectrum is a graph that shows each specific molecule by weight and how much of each molecule is present. Mass Spectrometer measure mass/charge ratio of an ion. Tandem Mass Spectrometry mainly generates partial N and C-terminal peptides. Spectrum consists of different ion types because peptides can be broken in several places. Tandem Mass Spectrometer further breaks the peptides down into fragment ions and measures the mass of each piece. The advantages of tandem mass spectrometry are the sequences that are not necessarily in the database and an additional similarity search step using these sequences may identify the related proteins in the database.
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Journal of Analytical & Bioanalytical Techniques, Journal of Bioanalysis & Biomedicine, Journal of proteome research, The American Society for Mass Spectrometry, International Journal of Mass Spectrometry, Royal Society of Chemistry
MALDI is that the abbreviation for Matrix Assisted Laser Desorption/Ionization. The sample for MALDI is uniformly mixed in an exceedingly lots of abundance of matrix. The matrix absorbs the ultraviolet tlight of wave length 337nm of nitrogen optical maser light and converts it to heat energy. In MALDI small a part of the matrix heats in many nano seconds and is volatilized along with the sample. Ions with same m/z ratio but higher kinetic energy penetrate deeper into the reflector, delaying their time of arrival at the reflector relative to the slower low-energy ions. The main advantages of MALDI includes used for study of polymers, proteins, peptides, Improved resolution, increase in mass accuracy, matrix disperses large amounts of energy absorbed by the laser, minimizes fragmentation of the molecule and permits analysis of molecular weight over 10,000 Da.
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Journal of Glycomics & Lipidomics, Journal of Chromatography & Separation Techniques, Journal of Analytical & Bioanalytical Techniques, Journal of Medical Microbiology, Medical Mycology, American Society for Mass Spectrometry
Protein purification is a series of processes to isolate protein from a complex mixture (cells, tissues or whole organisms) to one or a few proteins. Protein purification mainly depends on the structure and interactions of the protein of interest however thousands of proteins of each displaying unique characteristics. Protein purification is essential for a host of biochemical applications. It is the most important to develop a strategy for purification that delivers the correct yield, purity and activity needed for downstream applications. Primary steps for protein purification are extraction, precipitation/differential solubilization and ultracentrifugation.
Protein purification strategy consist one or more chromatographic steps like size exclusion chromatography, separation based on charge or hydrophobicity (hydrophobic interaction chromatography, ion exchange chromatography, Free-flow Electrophoresis), affinity chromatography(Metal binding, immunoaffinity chromatography, Purification of a tagged protein), HPLC methods.
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Journal of Bioanalysis & Biomedicine, Journal of Analytical & Bioanalytical Techniques, Protein Expression and Purification, Recombinant protein expression and purification.
Fourier transform mass spectrometry is the key performance characteristics of fourier transform-based mass spectrometry, mass accuracy and resolution are presented in the view of how they impact the interpretation of measurements in proteomic applications. The motion of ions in a Fourier Transform Mass Spectrometry analyzer can understand by the magnetic and electric fields present in the FTMS analyzer cell. The FTMS experiment is a series of events like ionization, excitation and detection that occur in sequence. Fourier transformation of the time domain signal results in the frequency domain FT-ICR signal which, on the basis of the inverse proportionality between frequency and m/z ratio, can be converted to a mass spectrum. The ions are to be detected, with a selected m/z ratio, absorb maximum energy through the effect of a high-frequency field and a constant magnetic field perpendicular to it. Maximum energy is gained by ions that satisfy the cyclotron resonance condition and as a result these are separated from ions of different mass/charge. The advantages of fourier transform mass spectrometry includes High mass resolution, accuracy of mass determination and structure-specific fragmentation.
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Journal of Proteomics & Bioinformatics, Journal of Pharmacogenomics & Pharmacoproteomics, Journal of Chromatography & Separation Techniques, Industrial Chemistry: Open Access, Journal of Chromatographic Science, Chromatography Research International and Journal of Liquid Chromatography & Related Technologies
Affinity Purification is a method of separating biochemical mixtures based on a highly specific interaction such as that between antigen and antibody, enzyme and substrate, or receptor and ligand. Most purification methods, however, involve some form of chromatography whereby molecules in solution are separated based on differences in chemical or physical interaction with a stationary material. Gel filtration (size-exclusion chromatography or SEC) uses a porous resin material to separate molecules based on size. In ion exchange chromatography, molecules are separated according to the strength of their overall ionic interaction with a solid phase material.
Affinity chromatography is unique purification technology. Affinity Purification is the only technique that enables the purification of biomolecule based on the biological function or individual chemical structure. Purification will be time-consuming, difficult or even impossible using other techniques can often be easily achieved with affinity chromatography. The technique can be used to separate active biomolecules from denatured or functionally different forms, to isolate pure substances present at low concentration in large volumes of crude sample and also to remove specific contaminants.
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Journal of Chromatography & Separation Techniques, Analytical & Bioanalytical Techniques Journal, Bioanalysis & Biomedicine Journal, Protein Expression and Purification, Proteome Research, Biotechnology Journal.
Gas chromatography is an analytical separation techniques used to analyze volatile substances in the gas phase or in a gaseous mixture at high temperatures. Gas chromatography can be used for both qualitative and quantitative analysis. Based on stationary phase gas chromatography can be divided mainly into as Gas - Solid Chromatography (GSC) and Gas - Liquid Chromatography (GLC). The main advantages of gas chromatography includes it gives very good separation, short analysis time, very less volume of sample for injection(µl), very high precision and quantitative analysis. The gas chromatography detect and quantitate alcohols in blood, aromatic compounds, flavors and fragrances, hydrocarbons, pesticides, herbicides and dioxins.
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Journal of Analytical & Bioanalytical Techniques, Journal of Chromatography & Separation Techniques, International Journal of Pharmaceutical Compounding, Journal of Chromatography, Journal of gas Chromatography, Journal of chemical education, International Journal of Analytical and Bioanalytical Chemistry
Liquid chromatography used to separate a sample into its individual part, or an analytical chromatographic technique used for the separation of molecules or ions which are dissolved in a mixture or a solvent. Different type of liquid chromatography includes Ion Exchange Chromatography, Partitioning Chromatography, Size Exclusion Chromatography, Supercritical Fluid Chromatography and Capillary Electrophoresis. Applications includes quantitative and qualitative analysis of low polarity compounds, measure picomoles of substance, peptide mass finger printing. The main application is in the drug development for peptide mapping, glycoprotein mapping, bio affinity screening, in vivo drug screening, metabolic stability screening, identification of metabolites, impurity identification, identification of degradant compounds, bioanalysis and quality control.
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Imaging Mass Spectrometry is a technology that combines most advanced analytical techniques for the analysis of biological molecules with spatial fidelity. An effective approach for imaging biological specimens in this way utilizes Matrix-Assisted Laser Desorption Ionization Mass Spectrometry. The mass-to-charge ratio of the ions are measured using a mass spectrometer over an ordered array of ablated spots. Imaging mass spectrum analysis (IMS) encompasses a spread of techniques that change the chemical imaging of analytes from atoms and little molecules to intact proteins directly from biological tissues. Imaging mass spectrometry is remodeling specific areas in research project with its distinctive combination of chemical and biological information. Innovations in instrumentation and imaging protocols can create this approach at several stages of the drug discovery method, as well as medical target screening and evaluating the distribution of drug and drug metabolites in cells and tissues.
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Journal of Bioanalysis & Biomedicine, Journal of Analytical & Bioanalytical Techniques, Journal of the American Society for Mass Spectrometry, Journal of Spectral Imaging, Journal of Pharmaceutical Analysis
Liquid-Liquid extraction is a method by which a compound is pulled from a solvent to another solvent where both the solvents are not miscible. The most common method of liquid-liquid extraction is performed using a separatory funnel. Other important liquid-liquid extraction processes are multistage countercurrent continuous processes, mixer-settlers, centrifugal extractors, extraction without chemical change.
The efficiency of a liquid liquid extraction can be enhanced by adding one or more extractants to the solvent phase. The extractant interacts with component increasing the capacity of the solvent for to recover the solute from the extract phase the extractant-solute complex has to be degraded. The major applications exist in the biochemical or pharmaceutical areas, for the separation of antibiotics and protein recovery. In the inorganic chemical field liquid-liquid extraction used to recover high-boiling components such as phosphoric acid, boric acid, and sodium hydroxide from aqueous solutions.
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Mass spectrometry in forensic studies is a technology provides a powerful tool for forensic studies. For forensic researchers investigating their samples for unknown compounds, drug metabolites, chemicals or hazards, novel psychoactive substances that have never been previously detected or characterized. The role of mass spectroscopy in forensic science may be characterised as either molecular or elemental analysis. comparatively little volatile nonionic molecules found in a very sort of forensic samples may be analyzed with electron and chemical ionization of single-stage mass analyzers that give relative molecular mass and structural data. Non-polar and polar molecules and their metabolites habitually found in biological matrices along with alternative analytes of forensic interest may be determined by using electrospray.
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Electron capture dissociation (ECD) is a new fragmentation technique used in Fourier transform ion cyclotron resonance mass spectrometry. Electron capture dissociation mass spectroscopy is complementary to traditional tandem mass spectrometry techniques. In biotechnology, the main area of electron capture dissociation application is the top-down verification of DNA-predicted protein sequences. The main applications of electron capture dissociation mass spectrometry includes in a wide range of biomolecules like peptides, proteins, carbohydrates, lipids, DNAs and RNAs.
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Deuterium exchange mass spectrometry is the mass spectrometry combined with hydrogen/deuterium. Deuterium exchange mass spectrometry is used to study the conformation and dynamics of proteins. The technique can be used in a comparative manner to identify changes in conformation and dynamics induced by ligand binding or point mutations. Deuterium exchange mass spectrometry is applicable in the areas of epitope mapping, protein-drug binding, protein-protein interactions, aggregation, effects of mutation on protein, formulations and stability testing. Hydrogen/deuterium trade mass spectrometry (H/DX-MS) is an effective device for mapping protein-protein interfaces and additionally distinguishing conformational and element annoyances in proteins. Furthermore, H/DX-MS empowers investigation of vast proteins at physiological fixations and gives understanding into the arrangement conduct of these buildings that can not be gathered from crystal structures. Hydrogen/deuterium trade mass spectrometry test used for ligand binding and the substrate identification.
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Protein folding by mass spectrometry is the key to the structure and function of the protein. Protein folding by mass spectrometry has come to the forefront as a powerful biophysical method, which can shed light both on the structure and dynamics of proteins. Ligand binding can change the conformational state of the protein, and changes in the amino acid sequence of the protein can change both the structure and the activity, which may cause to disease states. Apart from the charge state distribution, we can also study protein folding and dynamics by MS by exchanging deuterium onto the amide groups of the peptide backbone. The exchange of amide protons for deuterium happens on the millisecond timescale. Exchange is much faster than the rate of closing.
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Electrospray tandem mass spectrometry used to screen newborns for many rare inborn errors of metabolism. Electrospray tandem mass spectrometry is rapidly adopted for newborn screening programs to screen dried blood spots for >20 markers of disease in a single assay. The advancement of electrospray tandem mass spectrometry useful to screen infants for some uncommon inborn diseases. Many newborn disorders were examined by electrospray tandem mass spectrometry. Over the previous decade research facilities that test for metabolic issue have presented coupled mass spectrometry, which is more delicate, particular, solid and extensive than conventional measures into their infant screening projects.
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Liquid Chromatography Mass Spectrometry (LC/MS) is an analytical technique for identification, quantitation and mass analysis of wide variety of non-volatile, semi-volatile organic and inorganic compounds in a mixture. Using Liquid Chromatography mass spectrometry can identify a wide range of compounds from environmental contaminants to drug metabolites. Applications includes quantitative and qualitative analysis of low polarity compounds, measure picomoles of substance, peptide mass finger printing. The main application is in the drug development for peptide mapping, glycoprotein mapping, bio affinity screening, in vivo drug screening, metabolic stability screening, identification of metabolites, impurity identification, identification of degradant compounds, bioanalysis and quality control.
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Gas chromatography mass spectrometry (GC/MS) is a technique that combines the features of gas chromatography and mass spectrometry by which complex mixtures of chemical substances may be separated, identified and quantified. The main advantages of gas chromatography mass spectrometry which gives very good separation, short analysis time, very less volume of sample for injection(µl), very high precision and quantitative analysis. The gas chromatography detect and quantitate alcohols in blood, aromatic compounds, flavors and fragrances, hydrocarbons, pesticides, herbicides and dioxins.
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Protein mass spectrometry refers the use of mass spectrometry in studying the properties of proteins. Today mass spectrometry became an important tool for the characterization of proteins. Electrospray ionization and matrix-assisted laser desorption/ionization are the two important primary methods for ionization of whole proteins. Mass Spectrometer measure mass/charge ratio of an ion. Mass Spectrometry mainly generates partial N- and C-terminal peptides. Spectrum consists of different ion types because proteins can be broken in several places. The advantages of tandem mass spectrometry are, gets the sequences that are not necessarily in the database and an additional similarity search step using these sequences may identify the related proteins in the database.
Related journals of Protein Mass Spectrometry
Journal of Analytical & Bioanalytical Techniques, Journal of Chromatography & Separation Techniques, Industrial Chemistry: Open Access, Environmental Analytical Chemistry, International Journal of Mass Spectrometry, Journal of The American Society for Mass Spectrometry, European Journal of Mass Spectrometry
Mass spectrometry in medicine is the most important area to study for the development of medicines. Mass spectrometry is an analytic technique widely used many laboratories for the development of laboratory medicine. Various types of mass spectrometers are used in order to get improvements in assay performance that is occurring rapidly in areas such as toxicology, endocrinology, and biochemical genetics. Mass spectrometry is a diagnostic system with high specificity and a developing vicinity in research facility prescription. Different sorts of mass spectrometers are being utilized as a part of an expanding number of clinical research facilities around the globe. Mass spectrometry has contributed altogether to the development of restorative science in late decades, especially in connection to medication advancement, in-vitro diagnostics, dietary and natural drug.
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Pharmaceutics & Drug Delivery Research, Industrial Chemistry: Open Access, Pharmaceutics & Drug Delivery Research, Bioanalysis & Biomedicine, Journal of proteome research, The American Society for Mass Spectrometry, International Journal of Mass Spectrometry, Royal Society of Chemistry