X ray crystallography
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X-ray crystallography is a technique used for determining the atomic and molecular structure of a crystal, in which the crystalline atoms cause a beam of incident X-rays to diffract into many specific directions.
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X- ray Crystallograpy
X-ray crystallography is a technique used to determine the atomic and molecular structure of crystals. X-rays are directed at a crystal and the diffraction pattern produced is analyzed to reveal the crystal structure. This information can be used to construct a 3D electron density map and determine atomic positions. Some important applications of X-ray crystallography include determining the structures of proteins, viruses like HIV, and using this information to develop new drugs.
X ray crystallography
X-ray crystallography uses X-ray diffraction patterns from crystals to determine the atomic structure of molecules. Researchers first crystallize molecules and collect diffraction data by hitting the crystals with X-rays. Computers then analyze the diffraction patterns to deduce atomic positions and visualize molecular structures. This technique revealed structures of biological molecules like DNA and allows studying how environmental factors impact protein folding.
X-ray Crystallography & Its Applications in Proteomics
X-ray crystallography is a technique that uses X-rays to determine the atomic structure of crystals. It involves crystallizing molecules and bombarding them with X-rays, which produce a diffraction pattern. This pattern is used to deduce the molecular structure. X-ray crystallography has many applications in proteomics, including determining protein structures, studying protein interactions, and elucidating enzyme catalysis mechanisms. It provides atomic-level insights that advance understanding of protein function.
MALDI
MALDI is a soft ionization technique used in mass spectrometry to analyze large biomolecules. It works by co-crystallizing the analyte sample with a UV-absorbing matrix. A laser is used to excite the matrix, causing desorption and ionization of the analyte molecules. The ions are then analyzed by a mass spectrometer, typically a time-of-flight instrument. Careful sample preparation is important for reproducibility and performance. MALDI is widely used in pharmaceutical analysis and DNA sequencing due to its ability to characterize large organic and biomolecules.
X Ray Crystallography
X-Ray Crystallography is a technique used to determine the atomic and molecular structure of a crystal, in which the crystalline atoms cause a beam of incident X-rays to diffract into many specific directions.
Nmr spectroscopy
NMR spectroscopy is an analytical technique that uses the magnetic properties of certain nuclei, such as 1H and 13C, to characterize organic molecules. It was independently developed in the 1940s-1950s by groups at Harvard and Stanford, with Nobel Prizes awarded. There are two main types - 1H NMR studies hydrogen atoms and 13C NMR studies carbon atoms. The instrument uses a strong magnet to align nuclear spins, radio waves to excite them, and detectors to measure the radiofrequency energy emitted as the spins relax. NMR provides information about a molecule's structure through analysis of peak positions in its spectrum.
X-ray Crystallography
Including History, Principles, Various Methods, Instrumentation and Applications of X-ray Crystallography
Fluorescence spectrometry
fluorescence spectrometry, spectrofluorometry, basic principle , advantages, disadvantages , limitation, interference, luminescence, joblanski diagram, different parts of instruments, applications of it, phosphorescence, absorptions.
Recommended
X- ray Crystallograpy
X-ray crystallography is a technique used to determine the atomic and molecular structure of crystals. X-rays are directed at a crystal and the diffraction pattern produced is analyzed to reveal the crystal structure. This information can be used to construct a 3D electron density map and determine atomic positions. Some important applications of X-ray crystallography include determining the structures of proteins, viruses like HIV, and using this information to develop new drugs.
X ray crystallography
X-ray crystallography uses X-ray diffraction patterns from crystals to determine the atomic structure of molecules. Researchers first crystallize molecules and collect diffraction data by hitting the crystals with X-rays. Computers then analyze the diffraction patterns to deduce atomic positions and visualize molecular structures. This technique revealed structures of biological molecules like DNA and allows studying how environmental factors impact protein folding.
X-ray Crystallography & Its Applications in Proteomics
X-ray crystallography is a technique that uses X-rays to determine the atomic structure of crystals. It involves crystallizing molecules and bombarding them with X-rays, which produce a diffraction pattern. This pattern is used to deduce the molecular structure. X-ray crystallography has many applications in proteomics, including determining protein structures, studying protein interactions, and elucidating enzyme catalysis mechanisms. It provides atomic-level insights that advance understanding of protein function.
MALDI
MALDI is a soft ionization technique used in mass spectrometry to analyze large biomolecules. It works by co-crystallizing the analyte sample with a UV-absorbing matrix. A laser is used to excite the matrix, causing desorption and ionization of the analyte molecules. The ions are then analyzed by a mass spectrometer, typically a time-of-flight instrument. Careful sample preparation is important for reproducibility and performance. MALDI is widely used in pharmaceutical analysis and DNA sequencing due to its ability to characterize large organic and biomolecules.
X Ray Crystallography
X-Ray Crystallography is a technique used to determine the atomic and molecular structure of a crystal, in which the crystalline atoms cause a beam of incident X-rays to diffract into many specific directions.
Nmr spectroscopy
NMR spectroscopy is an analytical technique that uses the magnetic properties of certain nuclei, such as 1H and 13C, to characterize organic molecules. It was independently developed in the 1940s-1950s by groups at Harvard and Stanford, with Nobel Prizes awarded. There are two main types - 1H NMR studies hydrogen atoms and 13C NMR studies carbon atoms. The instrument uses a strong magnet to align nuclear spins, radio waves to excite them, and detectors to measure the radiofrequency energy emitted as the spins relax. NMR provides information about a molecule's structure through analysis of peak positions in its spectrum.
X-ray Crystallography
Including History, Principles, Various Methods, Instrumentation and Applications of X-ray Crystallography
Fluorescence spectrometry
fluorescence spectrometry, spectrofluorometry, basic principle , advantages, disadvantages , limitation, interference, luminescence, joblanski diagram, different parts of instruments, applications of it, phosphorescence, absorptions.
Affinity chromatography
This document discusses affinity chromatography, a technique used to separate biological molecules based on specific reversible interactions between a ligand attached to a matrix and the target molecule. It provides a brief history of affinity chromatography, outlines the basic principles and components including the matrix, spacer arm, and ligand. Examples of ligand-target pairs are given such as antigen-antibody and substrate-enzyme. Applications include purification of nucleic acids, antibodies, enzymes from mixtures. Advantages are high specificity and purity while disadvantages include cost and limited lifetime of the solid support.
X ray crystallography slideshare
X-ray crystallography is a technique that uses X-ray diffraction from a crystalline sample to determine its atomic structure. Crystals cause an incident X-ray beam to diffract into specific directions, and by measuring the angles and intensities of these diffracted beams, the electron density and positions of atoms in the crystal can be deduced. Key aspects of X-ray crystallography covered include the production of X-rays, the use of crystals to fix molecular conformations, different X-ray methods like diffraction, and applications like determining the structures of proteins and DNA.
Mass spectrometry basic principle & Instrumentation
Mass spectrometry is an analytical technique that identifies chemicals in a sample by measuring the mass-to-charge ratio and abundance of gas-phase ions. It works by bombarding molecule samples with electrons to produce positively charged ions, which are then separated by mass and detected. Mass spectra plots show the relative abundance of ions and are used to determine molecular structure and composition.
X ray crystellography
X-ray crystallography is a technique used to determine the atomic and molecular structure of crystals. It works by firing X-rays at a crystal and analyzing the diffracted rays. This allows researchers to construct a 3D model of the density of electrons within the crystal, revealing where atoms are located. Well-ordered protein crystals are required, as X-ray scattering from a single molecule would be too weak. Researchers grow crystals and collect diffraction data, which are then used to calculate atomic positions via Fourier transforms. This technique has determined over 85% of known protein structures and is invaluable for understanding functions at the molecular level.
X ray crystallography. presentation
This document provides an overview of x-ray crystallography. It discusses how x-rays are produced and diffracted by crystal structures, allowing researchers to determine atomic and molecular structures. The key techniques described are x-ray diffraction, Bragg's law for diffraction, and methods for collecting diffraction data like Laue photography, rotating crystal, and powder methods. These x-ray crystallography methods are useful for analyzing crystal structures and molecular structures of compounds.
fluroscence spectroscopy
Fluorescence spectroscopy involves using ultraviolet light to excite electrons in molecules, causing them to emit visible light. The emitted light has a longer wavelength than the absorbed light. Fluorimeters are used to measure fluorescence, exciting samples at an absorption wavelength and measuring emission at a longer fluorescence wavelength. Fluorescence spectroscopy is useful for applications like determining fluorescent drugs in formulations, carrying out limit tests for fluorescent impurities, and studying drug-protein binding in bioanalysis.
Spectrofluorimetry
Spectrofluorimetry involves the absorption of UV or visible radiation by a molecule, exciting it to a higher energy state. The molecule then relaxes and emits light of a longer wavelength. It is a sensitive technique that can detect low concentrations of organic and inorganic substances. Factors like conjugation, substituents, temperature, and oxygen presence affect fluorescence intensity. Instrumentation includes a light source, filters, sample cell, and detector. Applications include analysis of foods, pharmaceuticals, clinical samples, and natural products.
Autoradiography
Autoradiography is a bioanalytical technique used to visualize the distribution of radioactive substances in a biological sample. It involves placing a radioactive sample in contact with a photographic emulsion, which is then exposed over time. This allows the emulsion to capture the radioactive emissions and create an image showing where in the sample the radioactivity is located. Autoradiography provides high sensitivity and can be used to study the localization and movement of radioactive tracers in tissues, cells, and even biomolecules.
MS/MS, Tandem Mass Spectrometry
Tandem mass spectrometry is a technique that uses two or more mass spectrometers coupled together to analyze chemical samples. There are two types - tandem in time and tandem in space. Tandem in time uses one instrument to select an ion for fragmentation and then analyze the daughter ions. Tandem in space uses separate instruments where the first selects an ion for fragmentation in the interaction cell, and the second analyzes the product ions. Common fragmentation techniques include collision induced dissociation, electron capture dissociation, and photodissociation. Tandem MS can be used to obtain product ion spectra to identify compounds or perform selected reaction monitoring for quantitative analysis.
X - RAY CRYSTALLOGRAPHY TECHNIQUE
X-ray crystallography is a technique used to determine the atomic structure of crystals. It involves firing X-rays at a crystal and measuring the scattering pattern, which can reveal the positions of atoms within the crystal. Key apparatus include an X-ray source, filters and monochromators to produce a single wavelength beam, a diffractometer to rotate the crystal and detector, and an X-ray detector. The procedure involves growing crystals, collecting diffraction data, solving the crystal structure through methods like molecular replacement, and refining the structural model. X-ray crystallography is used to study biological molecules and materials that form crystals.
X ray Crystallography
X ray, invisible, highly penetrating electromagnetic radiation of much shorter wavelength (higher frequency) than visible light. The wavelength range for X rays is from about 10-8 m to about 10-11 m, the corresponding frequency range is from about 3 × 1016 Hz to about 3 × 1019 Hz.
Mass Spectroscopy
Mass spectroscopy is a technique used to analyze molecules. It involves ionizing molecules using electrons, accelerating the ions, and separating them based on their mass-to-charge ratio using electric or magnetic fields. The ions are then detected, producing a mass spectrum that is unique to each molecule and can be used to determine molecular structure. Mass spectroscopy requires only a small amount of sample and provides accurate molecular mass and elemental composition information. It is a destructive technique as the sample is consumed during ionization and fragmentation processes.
Mass spectroscopy, Ionization techniques and types of mass analyzers
Mass spectroscopy is a technique used to determine the molecular mass and elemental composition of a compound. It works by ionizing molecules using electron bombardment or chemical ionization and then separating the resulting ions based on their mass-to-charge ratio using electric and magnetic fields. The instrument consists of an ion source, a mass analyzer, and an ion detector. Common ion sources include electron impact, chemical ionization, and electrospray ionization, with each having advantages for different types of samples. The document provides detailed explanations of the basic principles and components of mass spectroscopy.
Mass spectroscopy
This document provides an overview of mass spectrometry. It begins with introductions to spectroscopy and mass spectroscopy. The basic principles of mass spectrometry are that molecules are ionized, the ions are accelerated and passed through electric and magnetic fields based on their mass-to-charge ratio, and detected. Common ionization techniques include electron ionization, chemical ionization, and desorption techniques like fast atom bombardment. The document describes different types of ions detected, such as molecular, fragment, and rearrangement ions. It also covers various mass analyzers used to separate ions such as magnetic sector, double focusing, and quadrupole analyzers.
Beer lamberts law
This document discusses Beer's law and Lambert's law, which describe how the intensity of light passing through an absorbing medium decreases exponentially with increasing thickness and concentration of the medium. It states that Beer's law relates the decrease in intensity to both the thickness and concentration, while Lambert's law relates it only to thickness. The document also describes deviations from the linear relationship predicted by these laws that can occur, including positive deviations where concentration changes have a greater than expected effect, and negative deviations where changes have a smaller effect. Possible causes of deviations, both instrumental and physicochemical, are outlined.
MALDI-TOF Mass Spectrometry
This presentation is about matrix-assisted laser desorption/ionization. It explains the sampling for TOF and its instrumentation.
Affinity chromatography
Affinity chromatography is a method used to purify biomolecules like proteins and nucleic acids based on specific interactions between the biomolecule and a ligand immobilized on a solid support. When a mixture is passed through the column, the target biomolecule will bind to the ligand while other molecules pass through. The bound biomolecule can then be separated by changing conditions like pH or introducing a competing molecule to displace it. Affinity chromatography offers highly specific purification of target molecules in a single step.
Analytical Ultracentrifugation
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Electron Spray Ionization (ESI) and its Applications
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Affinity chromatography ppt
Affinity chromatography is a method used to separate biological molecules like proteins and nucleic acids. It works by immobilizing a ligand with specific affinity for the target molecule on a chromatographic matrix or support. When a sample containing the target molecule is passed through the column, the target molecule will selectively bind to the ligand due to affinity interactions, while other molecules pass through. The target molecule can then be eluted from the column by changing buffer conditions in a process called affinity elution. Common applications of affinity chromatography include purifying enzymes, antibodies, and nucleic acids.
HPLC - High Performance Liquid Chromatography
The document discusses High Performance Liquid Chromatography (HPLC). It explains that HPLC is a type of liquid chromatography that uses pumps to force the mobile phase through a column packed with porous particles or beads under high pressure. This allows for effective separation of mixtures as the components elute from the column at different rates depending on their interactions with the stationary phase. The document provides details on the typical components of an HPLC system including the solvent delivery system, pumps, injector, columns, detectors, and data processing unit.
Bioluminescence
This document discusses bioluminescence in marine organisms. It explains that bioluminescence occurs through a chemical reaction between luciferin and luciferase that produces light. Many deep sea animals use bioluminescence for communication, attraction of mates, and camouflage. The light produced is typically in the blue and green spectrum as those wavelengths travel farthest underwater. While bioluminescence provides benefits to marine life, humans cannot glow because we lack the necessary biochemical processes and genes involved in light production.
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Affinity chromatography
This document discusses affinity chromatography, a technique used to separate biological molecules based on specific reversible interactions between a ligand attached to a matrix and the target molecule. It provides a brief history of affinity chromatography, outlines the basic principles and components including the matrix, spacer arm, and ligand. Examples of ligand-target pairs are given such as antigen-antibody and substrate-enzyme. Applications include purification of nucleic acids, antibodies, enzymes from mixtures. Advantages are high specificity and purity while disadvantages include cost and limited lifetime of the solid support.
X ray crystallography slideshare
X-ray crystallography is a technique that uses X-ray diffraction from a crystalline sample to determine its atomic structure. Crystals cause an incident X-ray beam to diffract into specific directions, and by measuring the angles and intensities of these diffracted beams, the electron density and positions of atoms in the crystal can be deduced. Key aspects of X-ray crystallography covered include the production of X-rays, the use of crystals to fix molecular conformations, different X-ray methods like diffraction, and applications like determining the structures of proteins and DNA.
Mass spectrometry basic principle & Instrumentation
Mass spectrometry is an analytical technique that identifies chemicals in a sample by measuring the mass-to-charge ratio and abundance of gas-phase ions. It works by bombarding molecule samples with electrons to produce positively charged ions, which are then separated by mass and detected. Mass spectra plots show the relative abundance of ions and are used to determine molecular structure and composition.
X ray crystellography
X-ray crystallography is a technique used to determine the atomic and molecular structure of crystals. It works by firing X-rays at a crystal and analyzing the diffracted rays. This allows researchers to construct a 3D model of the density of electrons within the crystal, revealing where atoms are located. Well-ordered protein crystals are required, as X-ray scattering from a single molecule would be too weak. Researchers grow crystals and collect diffraction data, which are then used to calculate atomic positions via Fourier transforms. This technique has determined over 85% of known protein structures and is invaluable for understanding functions at the molecular level.
X ray crystallography. presentation
This document provides an overview of x-ray crystallography. It discusses how x-rays are produced and diffracted by crystal structures, allowing researchers to determine atomic and molecular structures. The key techniques described are x-ray diffraction, Bragg's law for diffraction, and methods for collecting diffraction data like Laue photography, rotating crystal, and powder methods. These x-ray crystallography methods are useful for analyzing crystal structures and molecular structures of compounds.
fluroscence spectroscopy
Fluorescence spectroscopy involves using ultraviolet light to excite electrons in molecules, causing them to emit visible light. The emitted light has a longer wavelength than the absorbed light. Fluorimeters are used to measure fluorescence, exciting samples at an absorption wavelength and measuring emission at a longer fluorescence wavelength. Fluorescence spectroscopy is useful for applications like determining fluorescent drugs in formulations, carrying out limit tests for fluorescent impurities, and studying drug-protein binding in bioanalysis.
Spectrofluorimetry
Spectrofluorimetry involves the absorption of UV or visible radiation by a molecule, exciting it to a higher energy state. The molecule then relaxes and emits light of a longer wavelength. It is a sensitive technique that can detect low concentrations of organic and inorganic substances. Factors like conjugation, substituents, temperature, and oxygen presence affect fluorescence intensity. Instrumentation includes a light source, filters, sample cell, and detector. Applications include analysis of foods, pharmaceuticals, clinical samples, and natural products.
Autoradiography
Autoradiography is a bioanalytical technique used to visualize the distribution of radioactive substances in a biological sample. It involves placing a radioactive sample in contact with a photographic emulsion, which is then exposed over time. This allows the emulsion to capture the radioactive emissions and create an image showing where in the sample the radioactivity is located. Autoradiography provides high sensitivity and can be used to study the localization and movement of radioactive tracers in tissues, cells, and even biomolecules.
MS/MS, Tandem Mass Spectrometry
Tandem mass spectrometry is a technique that uses two or more mass spectrometers coupled together to analyze chemical samples. There are two types - tandem in time and tandem in space. Tandem in time uses one instrument to select an ion for fragmentation and then analyze the daughter ions. Tandem in space uses separate instruments where the first selects an ion for fragmentation in the interaction cell, and the second analyzes the product ions. Common fragmentation techniques include collision induced dissociation, electron capture dissociation, and photodissociation. Tandem MS can be used to obtain product ion spectra to identify compounds or perform selected reaction monitoring for quantitative analysis.
X - RAY CRYSTALLOGRAPHY TECHNIQUE
X-ray crystallography is a technique used to determine the atomic structure of crystals. It involves firing X-rays at a crystal and measuring the scattering pattern, which can reveal the positions of atoms within the crystal. Key apparatus include an X-ray source, filters and monochromators to produce a single wavelength beam, a diffractometer to rotate the crystal and detector, and an X-ray detector. The procedure involves growing crystals, collecting diffraction data, solving the crystal structure through methods like molecular replacement, and refining the structural model. X-ray crystallography is used to study biological molecules and materials that form crystals.
X ray Crystallography
X ray, invisible, highly penetrating electromagnetic radiation of much shorter wavelength (higher frequency) than visible light. The wavelength range for X rays is from about 10-8 m to about 10-11 m, the corresponding frequency range is from about 3 × 1016 Hz to about 3 × 1019 Hz.
Mass Spectroscopy
Mass spectroscopy is a technique used to analyze molecules. It involves ionizing molecules using electrons, accelerating the ions, and separating them based on their mass-to-charge ratio using electric or magnetic fields. The ions are then detected, producing a mass spectrum that is unique to each molecule and can be used to determine molecular structure. Mass spectroscopy requires only a small amount of sample and provides accurate molecular mass and elemental composition information. It is a destructive technique as the sample is consumed during ionization and fragmentation processes.
Mass spectroscopy, Ionization techniques and types of mass analyzers
Mass spectroscopy is a technique used to determine the molecular mass and elemental composition of a compound. It works by ionizing molecules using electron bombardment or chemical ionization and then separating the resulting ions based on their mass-to-charge ratio using electric and magnetic fields. The instrument consists of an ion source, a mass analyzer, and an ion detector. Common ion sources include electron impact, chemical ionization, and electrospray ionization, with each having advantages for different types of samples. The document provides detailed explanations of the basic principles and components of mass spectroscopy.
Mass spectroscopy
This document provides an overview of mass spectrometry. It begins with introductions to spectroscopy and mass spectroscopy. The basic principles of mass spectrometry are that molecules are ionized, the ions are accelerated and passed through electric and magnetic fields based on their mass-to-charge ratio, and detected. Common ionization techniques include electron ionization, chemical ionization, and desorption techniques like fast atom bombardment. The document describes different types of ions detected, such as molecular, fragment, and rearrangement ions. It also covers various mass analyzers used to separate ions such as magnetic sector, double focusing, and quadrupole analyzers.
Beer lamberts law
This document discusses Beer's law and Lambert's law, which describe how the intensity of light passing through an absorbing medium decreases exponentially with increasing thickness and concentration of the medium. It states that Beer's law relates the decrease in intensity to both the thickness and concentration, while Lambert's law relates it only to thickness. The document also describes deviations from the linear relationship predicted by these laws that can occur, including positive deviations where concentration changes have a greater than expected effect, and negative deviations where changes have a smaller effect. Possible causes of deviations, both instrumental and physicochemical, are outlined.
MALDI-TOF Mass Spectrometry
This presentation is about matrix-assisted laser desorption/ionization. It explains the sampling for TOF and its instrumentation.
Affinity chromatography
Affinity chromatography is a method used to purify biomolecules like proteins and nucleic acids based on specific interactions between the biomolecule and a ligand immobilized on a solid support. When a mixture is passed through the column, the target biomolecule will bind to the ligand while other molecules pass through. The bound biomolecule can then be separated by changing conditions like pH or introducing a competing molecule to displace it. Affinity chromatography offers highly specific purification of target molecules in a single step.
Analytical Ultracentrifugation
Includes concepts of Centrifugation; Types of centrifugations; Analytical Ultracentrifugation in detail; Marker enzymes overview
Electron Spray Ionization (ESI) and its Applications
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Affinity chromatography ppt
Affinity chromatography is a method used to separate biological molecules like proteins and nucleic acids. It works by immobilizing a ligand with specific affinity for the target molecule on a chromatographic matrix or support. When a sample containing the target molecule is passed through the column, the target molecule will selectively bind to the ligand due to affinity interactions, while other molecules pass through. The target molecule can then be eluted from the column by changing buffer conditions in a process called affinity elution. Common applications of affinity chromatography include purifying enzymes, antibodies, and nucleic acids.
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Mass spectrometry basic principle & Instrumentation
Mass spectrometry basic principle & Instrumentation
Mass spectroscopy, Ionization techniques and types of mass analyzers
Mass spectroscopy, Ionization techniques and types of mass analyzers
Electron Spray Ionization (ESI) and its Applications
Electron Spray Ionization (ESI) and its Applications
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Bioluminescence
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Liquid chromatography principles
Liquid chromatography is a technique that separates molecules using a liquid mobile phase and solid stationary phase. Components in a mixture interact to different degrees with the stationary phase and separate as they pass through the column. The composition of the mobile phase is typically changed to alter interactions and elute components in a particular order. Key aspects of liquid chromatography include column equilibration, sample loading, washing, gradient or stepwise elution, and column regeneration between uses. Resolution, yield, integrity and purity of separated components must be considered.
Gas chromatography GC
A separation technique in which the mobile phase is a gas. Gas chromatography is always carried out in a column.
Separating mixtures of gases or volatile materials based primarily on their physical properties.
X ray powder diffraction
This document discusses X-ray diffraction, including its basic principles and applications. It describes how X-rays are produced via bombardment of a metal target, and how they interact with crystal structures to produce diffraction patterns. Bragg's law is explained as relating the diffraction angle to the wavelength and interplanar spacing. The key methods of X-ray diffraction analysis are powder diffraction and single crystal diffraction using Bragg spectrometers or rotating crystal cameras. Its applications include mineral identification, crystalline structure determination, and measurement of crystallite size.
Application of radio isotopes
Radioisotopes are used for both diagnosis and treatment in medicine. For diagnosis, radionuclides are combined with other elements and injected or taken orally, then detected externally to form images of areas like organs and blood flow. Positron emission tomography is commonly used in oncology. Technetium-99m is widely used to image bones, heart, lungs, liver, and other organs. For treatment, radioisotopes are used to treat conditions like hyperthyroidism, thyroid cancer, and blood disorders. Cobalt-60 and phosphorus-32 were formerly used to externally radiotherapy and treat polycythemia vera.
Reverse phase chromatography
Reverse phase chromatography is a technique where the binding of solutes to a hydrophobic stationary phase occurs via hydrophobic interactions. It uses a stationary phase with hydrophobic ligands chemically bonded to a solid support. Polar mobile phases are used to elute retained solutes from the column. Key parameters that affect separation include the pH, ionic strength, and polarity of the mobile phase, use of gradients or isocratic elution, column length, and addition of ion-pairing agents. Reverse phase chromatography is commonly used to purify biomolecules like proteins, peptides, and nucleic acids.
X ray
X-ray crystallography is used to determine the atomic structure of crystals. X-rays are directed onto a crystal and cause the atoms to diffract the x-rays into specific directions. By measuring the angles and intensities of the diffracted beams, researchers can construct a three-dimensional model of the electron density within the crystal and determine the positions of the atoms and their chemical bonds. Crystals are used because they help amplify the diffraction signal. The technique involves obtaining a suitable crystal, exposing it to x-rays to create a diffraction pattern, and then using the data and complementary information to computationally produce an atomic model of the crystal structure.
Radiolabeling technique
Radiolabeling is a technique that uses radioactive isotopes to track molecules. Isotopes like 32P and 35S emit radiation that can be detected. Nucleic acids can be labeled isotopically by incorporating these radioactive nucleotides. Two common detection methods are autoradiography, which uses photographic film to detect radiation, and scintillation counting, which detects light pulses from samples exposed to scintillants.
Introduction and principle of glc, hplc
This document provides an introduction and overview of gas liquid chromatography (GLC) and high performance liquid chromatography (HPLC). It defines chromatography as a technique that separates components of a mixture based on differences in affinity for a stationary and mobile phase. GLC uses an inert gas as the mobile phase and a liquid stationary phase, while HPLC uses high pressure to push a liquid mobile phase through a column. The document describes the basic instrumentation, principles, and applications of these techniques.
pH meter design and working principle
A pH meter measures the concentration of hydrogen ions in a solution to determine if it is acidic or alkaline. It works by measuring the potential difference between a glass electrode that senses the hydrogen ions and a reference electrode in contact with a reference solution. The glass electrode contains a special glass bulb that allows hydrogen ions to interact with it, changing the electrochemical potential. This potential difference is measured by the pH meter and converted to a pH value. A silver chloride electrode is commonly used as the reference electrode due to its stable and reproducible reaction.
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Radioisotopes in biology
This document discusses the history and applications of radioisotopes in biology. It begins with an introduction to radioisotopes and radioactive decay. Key discoveries in radioactivity from the 1890s are mentioned. The document then discusses the structure of atoms and isotopes, as well as the different types of radioactive decay. Applications of radioisotopes in biology are summarized, including radiotracing of metabolic pathways, radioimmunoassays, gene expression studies using radiolabeled probes, and medical uses like PET imaging and radiation therapy. Some disadvantages of radioisotopes are noted, as well as their significant role in research and medicine.
Ion exchange chromatography
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Ion Exchange Chromatography, ppt
Ion exchange chromatography is a technique used to separate mixtures of similarly charged ions using an ion exchange resin. The resin works by reversibly exchanging ions between those present in the solution and the resin. There are different types of ion exchange resins classified by their chemical nature (strong/weak cation or anion exchangers) and source (natural or synthetic). Successful ion exchange requires the resin to be chemically stable, insoluble, sufficiently cross-linked, and contain exchange groups.
X ray diffraction
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Gas chromatography . ppt
Gas chromatography is a technique used to separate and analyze volatile compounds. It works by injecting a sample into a column through which an inert gas flows, carrying the separated components out at different rates depending on their interactions with the stationary phase coating the column. The separated components are detected to produce a chromatogram showing peaks that can be analyzed to determine the identity and quantity of each component in the original sample.
Paper chromatography(final)
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Ion exchange Chromatography
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X ray crystallography
X-ray crystallography is a technique used to determine the atomic and molecular structure of crystals. When a beam of X-rays hits a crystal, the crystal causes the beam to diffract into specific directions. From this diffraction pattern, the electron density within the crystal can be determined, allowing the mean positions of atoms to be found. Bragg's law relates the angles and wavelengths of incident and diffracted X-ray beams to the spacing of crystal planes. X-ray crystallography instruments consist of an X-ray source, wavelength selector, sample holder, and detector. This technique is used in applications such as determining protein and viral structures, material science, and polymer characterization.
Crystallography.pptx
X-ray crystallography is a technique used to determine the atomic and molecular structure of crystals. An X-ray beam is directed at a crystal and causes the beam to diffract into specific directions. The angles and intensities of the diffracted beams are used to produce a 3D image of electron density within the crystal. This allows determining the positions of atoms and chemical bonds within the crystal. There are several methods of X-ray crystallography including single crystal diffraction, powder diffraction, and rotating crystal techniques. Each method uses X-ray diffraction patterns to analyze crystal structure.
x ray crystallography & diffraction
X-rays introduction, why xrays, why crystals, Xray diffraction, Bragg's law, Interference, Crystal lattice , Instrumentation of xray crystallography, Production of Xrays, Monochromator, Types of Monochromator, Interference filters, Crystal monochromator, xray diffration methods - single crystal, rotating crystal, powder method, Applications of xray crystallography
X ray diffraction
X-ray diffraction is a technique that uses X-rays to determine the atomic and molecular structure of crystals. When X-rays hit a crystal, they cause the atoms to diffract into specific patterns determined by Bragg's law. By analyzing these diffraction patterns, information about the crystal structure such as lattice parameters and spacing between atomic planes can be determined. Common applications of XRD include identifying materials and determining their purity, structure, and properties.
X ray crystallography to visualize protein structure.
This ppt discusses in detail the process of X ray Crystallography.
Made by the following 3rd year Bs-Ms students of IISER Kolkata:
B Sri Sindhu
Rasiwala Hassan Shabbir
Ritam Samanta
Himanshu Gupta
Sakshi Ajay Shrisath
Aditya Borkar
Diana Denzil Fernandez
Neha Kumari
.Sowmya
Anjali Mohan
Debanjana Mondal
Aanandita Gope
Shruti Santosh Sail
x-raycrystallography-200619161039-200622085916.pptx
X-ray crystallography uses X-rays to determine the atomic structure of crystals. It works by firing X-rays at crystalline samples and analyzing the diffraction patterns. This allows researchers to visualize protein structures and identify unknown crystal structures. The key steps are obtaining a suitable crystal sample, exposing it to X-rays, and computationally analyzing the diffraction data to produce an atomic model of the crystal structure. Common applications include determining molecular structures, characterizing polymers, and assessing the crystallinity and degradation of materials.
99995067.ppt
X-ray diffraction is a technique used to analyze the crystal structure of materials. Wilhelm Röntgen discovered X-rays in 1895, and Max von Laue discovered X-ray diffraction by crystals in 1912. Bragg's law, discovered in 1913, forms the basis for analyzing diffraction patterns to determine crystal structures. While traditionally useful, X-ray diffraction faces challenges in analyzing nanostructures due to their lack of long-range order and increased defects. Advances in detection technology and techniques have helped make X-ray diffraction applicable to characterizing nanomaterials.
X ray crystallography
X-ray crystallography is a scientific technique used to determine the atomic and molecular structure of crystals. When x-rays strike a crystal, the beam diffracts into specific directions. This diffraction pattern can be analyzed to reveal the nature and structure of the crystal lattice. Bragg's law defines the relationship between x-ray wavelength, diffraction angle, and interplanar spacing and is used to calculate crystal structures from diffraction data. X-ray crystallography is widely used to determine protein structures and has applications in pharmaceuticals, materials science, and other fields.
X ray crystallography
X-ray crystallography uses x-ray diffraction patterns to determine the atomic structure of crystals. X-rays are produced using an x-ray tube and passed through a monochromator to produce a single wavelength. The x-rays are then directed at a crystal sample, which causes the beams to diffract into specific directions based on the crystal structure. Detectors measure the intensities and angles of the diffracted beams, which are used to reconstruct the three-dimensional electron density and atomic positions in the crystal. X-ray crystallography has applications in determining crystal structures, polymer characterization, and analyzing materials.
X ray crystallography
X-ray crystallography is a technique used to determine the arrangement of atoms in crystalline solids by using X-rays. When an X-ray beam hits a crystal, it causes the beam to diffract in specific directions. By measuring the angles and intensities of these diffracted beams, a crystallographer can produce a 3D image of electron density within the crystal. X-ray crystallography uses an X-ray diffractometer containing an X-ray source, monochromator, collimator, goniometer, detector and other parts. It has wide applications in fields like medicine, molecular biology, materials science and more to determine molecular structures.
X ray powder diffraction
X-ray powder diffraction is a technique used to analyze the crystal structure of materials. Finely powdered samples are bombarded with X-rays, and the resulting diffraction pattern is analyzed. Each material produces a unique pattern that can be used for identification. The instrument works by generating monochromatic X-rays that diffract off the sample, producing concentric cones. The pattern is recorded and analyzed to determine properties like unit cell dimensions. Common applications include phase identification, purity analysis, and structure determination of minerals, compounds, and alloys. The technique is rapid, non-destructive, and requires only small sample amounts.
X- ray crystallography
X-ray crystallography uses X-rays to determine the atomic structure of crystals. Crystals are bombarded with X-rays, which diffract upon contact with the atoms in the crystal. The angles and intensities of the diffracted X-rays are measured to deduce the positions of atoms in the crystal. This technique is useful for visualizing protein structures and identifying unknown crystal structures. It involves growing a crystal, exposing it to X-rays, and computationally analyzing the diffraction pattern to produce an atomic model of the crystal structure. X-ray crystallography has applications in characterizing polymers, assessing metal fatigue, and soil classification.
X- ray crystallography, Shriyansh Srivastava, M.Pharm (Department of Pharmaco...
X-ray crystallography uses X-rays to determine the atomic and molecular structure of crystals. Wilhelm Röntgen discovered X-rays in 1895. X-rays are produced when high velocity electrons collide with a metal target. X-ray crystallography works by firing a beam of X-rays at crystalline solids and observing the diffraction pattern of scattered X-rays. Bragg's law describes the conditions under which constructive interference of X-rays occurs and can be used to determine crystal structures. Common methods include rotating crystal, powder diffraction, and using detectors like photographic film, Geiger-Müller counters, or scintillation counters. X-ray crystallography has applications in determining protein structures and identifying
some active beamlines properties
The document discusses various active beamlines at synchrotron facilities around the world. It describes what a beamline is and the typical segments it contains, including optics cabins which house components like beam position monitors, filters, slits, and primary optics like monochromators and mirrors. Specific beamlines are highlighted, such as the PROXIMA-1 beamline at SOLEIL, which is used for macromolecular crystallography to determine protein structures. Detectors play an important role in experiments like X-ray diffraction.
X-RAY CRYSTALLOGRAPHY.pptx
X-ray Crystallography is a scientific method used to determine the arrangement of atoms of a crystalline solid in three dimension. It is based on x ray diffraction. Reveals structure of a crystal at atomic level.
XRD BY SATYAM.pdf
This document discusses X-ray diffraction (XRD), including its principle, concept, instrumentation, methods, and applications. XRD is a technique used for phase identification of crystalline materials based on constructive interference of X-rays diffracted from a crystalline sample. It can provide information on unit cell dimensions. The key components of an XRD instrument are an X-ray tube, sample holder, detector, and analyzer. Common methods include Bragg's method, Laue's method, and powder diffraction. XRD has applications in determining crystal structure, polymer characterization, and particle size analysis.
Dipti_X ray crystallography (1).pptx
X-ray crystallography is the experimental science determining the atomic and molecular structure of a crystal, in which the crystalline structure causes a beam of incident X-rays to diffract into many specific directions. By measuring the angles and intensities of these diffracted beams, a crystallographer can produce a three-dimensional picture of the density of electrons within the crystal. From this electron density, the mean positions of the atoms in the crystal can be determined, as well as their chemical bonds, their crystallographic disorder, and various other information.
Analytical instrument
In mineral science, there are several analytical instruments used for various purpose, viz…
Scanning electron microscopy
X-ray diffraction
Transmission electron microscopy
X-ray fluorescence
Flame atomic absorption spectroscopy
Electron microprobe analysis
Secondary ion mass spectrometry
Atomic force microscopy
X ray crystallography
X-ray crystallography is a method to determine the arrangement of atoms in a crystal by firing X-rays at the crystal. The X-rays cause the beam to diffract in specific directions, and from the angles and intensities of these diffracted beams, a three-dimensional picture of electron density within the crystal can be produced. X-ray crystallography uses the uniform diffraction of crystals to determine the structure of molecules by hitting them with an X-ray beam and analyzing the resulting diffraction pattern. It has applications in studying materials like salts, metals, minerals, and biological molecules.
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X ray crystallography to visualize protein structure.
X ray crystallography to visualize protein structure.
x-raycrystallography-200619161039-200622085916.pptx
x-raycrystallography-200619161039-200622085916.pptx
X- ray crystallography, Shriyansh Srivastava, M.Pharm (Department of Pharmaco...
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X ray crystallography
- 2. Index -History -x-ray -Introduction -Instrumentation x-ray source monochromatic calorimeter Goniometry photographic plat film detector -Principal -Working -Application -Reference
- 3. History x-ray crystallography was discovered by Johns kaplae in 17th century.
- 4. X ray An electromagnetic wave of high energy and very short wavelength (between ultraviolet light and gamma ray).which is able to pass through many materials opaque to light.
- 5. Introduction 1. X-ray is the study of any crystalline structure of bio molecules using x-ray. 2.s It is widely use in biological science for studying structure of biological molecule such as protein, antibiotics, fats, DNA, RNA.
- 6. Properties 1.X-ray travel in straight lines. 2.x-ray are electrically neutral. 3.x-ray are polynergetic and heterogonous. 4.x-ray are invisible ray.
- 7. Instruments The instrument used in x-ray crystallography is know as x- ray diffractometer and content following part: 1. X-ray source 2. Monochromater 3. Calorimeter 4. Goneometer 5. Photographic plate film 6. Detector
- 8. X-ray source the x-ray most common source of x-ray is an x-ray tube . The tube is evacuated and contains a copper block with a metal target anode, and a tungsten filament cathode with a high voltage between them.
- 9. Monochromater It act as x-ray filter which remove unwanted rays, generally12-24 am- strong ray has been in x-ray. The name is form the Greek roots mono-” single", and chroma-”colour”.
- 10. Collimator This comprises of 2 closely packed metal plate which are 0.3mm apart from each other. The x-ray beam originate from x-ray source passes through this gap and follow single line path.
- 11. Goniometry It is device on which crystal whose structure is to be determine has been mounted. This device spin slowly in according to crystal which to rotate on constant speed. This place between collimator and photo plate.
- 12. Photo plate film As the name suggest this plate capture the diffraction rays of crystal. The light-sensitive emulsion of silver salts was coated on a glass plate ,typically thinner than common window glass ,instead of a clear plastic film .
- 13. Detector The captured data has been send to computer for further processing by detector where 3D structure of crystal gets develop.
- 14. Principle The principle is based on principle of diffraction 1. The crystal is made to strike against x-ray beam. 2. Due to striking the atoms present in crystal diffracts the x-ray beam into different direction. 3. The angel and intensity of this diffraction rays is analog to spatial arrangement of atom in crystal. 4. By studying these angle, the 3D structure of any crystal can be determine. 5.X-rays are generated by bombarding electrons on an metallic anode.
- 15. Working
- 16. Protein Sample for Crystallization: Pure and homogenous (identified by SDS-PAGE, Mass Spec. etc.) Properly folded Stable for at least few days in its crystallization condition (dynamic light scattering) Conditions Effect Crystallization - pH (buffer) - Protein Concentration - Salt (Sodium Chloride,AmmoniumChloride etc.) - Precipitant - Detergent - Temperature - Size and shape of the drops - Pressure
- 17. Application 1. The various atomic arrangement present in graphite diamond can be study using x-ray diffraction. 2. the lattice structure of crystal can be revealed using x-ray diffraction 3. protein, antibody, DNA, RNA, lipids and other bio molecules structure can be study 4. bond such as covalent bonds and ionic that exist between molecule can be study. 5. the molecular structure of penicillin, vitamin B12, insulin etc can be determine using x-ray diffraction.
- 18. Reference Avinash Upadhyay, Himalaya publishing house, Biophysical Chemistry, Fourth edition, chapter 11, , pg no. 523-535. http://www.google.com http://www.wikipedia.com
- 19. Thank you