The document provides an introductory overview of mass spectrometry, explaining that it works by ionizing sample molecules, separating the ions by their mass-to-charge ratio using different types of mass analyzers, and detecting the ions to produce a mass spectrum. It discusses the various applications of mass spectrometry in areas like pharmaceutical analysis, biomolecule characterization, and environmental and forensic analysis. The document also describes the basic components and working principles of mass spectrometers, including how they ionize samples, analyze ions, and generate mass spectra.
Mass spectrometry involves ionizing molecule samples and then measuring their mass-to-charge ratios. The samples are bombarded with electrons to produce molecular ions, which then fragment into product ions. These ions are separated based on their mass-to-charge ratios and detected, producing a mass spectrum that shows the abundances of each ion. This spectrum provides structural information about the precursor molecule and can be used to identify unknown compounds. Mass spectrometry is widely applied across many scientific fields including pharmaceutical analysis, environmental testing, and forensics.
Mass analyzers separate ionized molecules based on their mass-to-charge ratios. The main types are quadrupole, time-of-flight, magnetic sector, quadrupole ion trap, and ion cyclotron resonance. A quadrupole uses oscillating electric fields to selectively transmit ions through four rods. Time-of-flight separates ions by their time of flight through a field-free region, with lighter ions arriving first. Magnetic sector analyzers use magnetic and electric fields to curve ion trajectories based on m/z.
Mass spectrometry is a technique that converts a sample to gas-phase ions which are then separated by mass and charge. It involves ionization of the sample using electron bombardment or other methods, mass analysis using magnetic or electric fields to separate ions, and detection of ion abundances. Mass spectrometry can be used to determine molecular masses and obtain structural information through fragmentation patterns.
This document provides an overview of mass spectrometry. It discusses the brief history of mass spectrometry from 1913 to 2002. It then summarizes the basic principles and components of mass spectrometers, including sample inlet systems, ion sources like electron impact and electrospray ionization, mass analyzers like quadrupole and time-of-flight, detectors, and applications in fields like pharmaceuticals, clinical work, environment and biotechnology. The document aims to introduce readers to mass spectrometry through examining its origins, instrumentation, and uses.
This document discusses various ionization techniques used in mass spectrometry. It begins with an introduction to mass spectrometry and its basic principles. It then describes several ionization sources including gas phase sources like electron impact ionization and chemical ionization, and desorption sources like electrospray ionization, matrix-assisted laser desorption/ionization, and fast atom bombardment. The document proceeds to provide more detailed explanations of specific ionization techniques like electrospray ionization, atmospheric pressure chemical ionization, atmospheric pressure photoionization, matrix-assisted laser desorption ionization, and fast atom bombardment. It concludes with references used in the document.
Interfaces in chromatography [LC-MS, GC-MS, HPTLC, LC, GC]Shikha Popali
THE INTERFACES OF CHROMATOGRAPHY INCLUDES THE CHROMATOGRAPHY CRITEREA WHERE THE DIFFERENT CHROMATOGRAPHY ARE EXPLAINED IN DETAIL WITH PRACTICAL EXAMPLES AND THEIR IMAGES.
Nuclear magnetic resonance (NMR) spectroscopy exploits the magnetic properties of certain nuclei to study the physical, chemical, and biological properties of matter. NMR provides detailed information about molecular structure through analysis of spectra. 1H NMR spectra reveal the number and environment of hydrogen atoms in a molecule based on signal frequency (chemical shift) and splitting patterns. 13C NMR spectra similarly provide information about carbon atoms, though the low natural abundance of 13C and long relaxation times make these spectra less sensitive. NMR spectroscopy is a powerful nondestructive analytical technique for elucidating molecular structure.
Mass spectrometry involves ionizing molecule samples and then measuring their mass-to-charge ratios. The samples are bombarded with electrons to produce molecular ions, which then fragment into product ions. These ions are separated based on their mass-to-charge ratios and detected, producing a mass spectrum that shows the abundances of each ion. This spectrum provides structural information about the precursor molecule and can be used to identify unknown compounds. Mass spectrometry is widely applied across many scientific fields including pharmaceutical analysis, environmental testing, and forensics.
Mass analyzers separate ionized molecules based on their mass-to-charge ratios. The main types are quadrupole, time-of-flight, magnetic sector, quadrupole ion trap, and ion cyclotron resonance. A quadrupole uses oscillating electric fields to selectively transmit ions through four rods. Time-of-flight separates ions by their time of flight through a field-free region, with lighter ions arriving first. Magnetic sector analyzers use magnetic and electric fields to curve ion trajectories based on m/z.
Mass spectrometry is a technique that converts a sample to gas-phase ions which are then separated by mass and charge. It involves ionization of the sample using electron bombardment or other methods, mass analysis using magnetic or electric fields to separate ions, and detection of ion abundances. Mass spectrometry can be used to determine molecular masses and obtain structural information through fragmentation patterns.
This document provides an overview of mass spectrometry. It discusses the brief history of mass spectrometry from 1913 to 2002. It then summarizes the basic principles and components of mass spectrometers, including sample inlet systems, ion sources like electron impact and electrospray ionization, mass analyzers like quadrupole and time-of-flight, detectors, and applications in fields like pharmaceuticals, clinical work, environment and biotechnology. The document aims to introduce readers to mass spectrometry through examining its origins, instrumentation, and uses.
This document discusses various ionization techniques used in mass spectrometry. It begins with an introduction to mass spectrometry and its basic principles. It then describes several ionization sources including gas phase sources like electron impact ionization and chemical ionization, and desorption sources like electrospray ionization, matrix-assisted laser desorption/ionization, and fast atom bombardment. The document proceeds to provide more detailed explanations of specific ionization techniques like electrospray ionization, atmospheric pressure chemical ionization, atmospheric pressure photoionization, matrix-assisted laser desorption ionization, and fast atom bombardment. It concludes with references used in the document.
Interfaces in chromatography [LC-MS, GC-MS, HPTLC, LC, GC]Shikha Popali
THE INTERFACES OF CHROMATOGRAPHY INCLUDES THE CHROMATOGRAPHY CRITEREA WHERE THE DIFFERENT CHROMATOGRAPHY ARE EXPLAINED IN DETAIL WITH PRACTICAL EXAMPLES AND THEIR IMAGES.
Nuclear magnetic resonance (NMR) spectroscopy exploits the magnetic properties of certain nuclei to study the physical, chemical, and biological properties of matter. NMR provides detailed information about molecular structure through analysis of spectra. 1H NMR spectra reveal the number and environment of hydrogen atoms in a molecule based on signal frequency (chemical shift) and splitting patterns. 13C NMR spectra similarly provide information about carbon atoms, though the low natural abundance of 13C and long relaxation times make these spectra less sensitive. NMR spectroscopy is a powerful nondestructive analytical technique for elucidating molecular structure.
MALDI...
This Presentation Contain following...
#Introduction
#Matrix and examples
#Considerations of Matrix Material
#MALDI Sample Preparation
#Mechanism of MALDI
#Mass Spectrometer
#Reproducibility and Performance
#Uses of MALDI
#Conclusion
#References
Thanks For Help and Guidance of Mr. D.V. Mahuli Sir and Mr. V.T. Pawar Sir
This document provides an overview of different ionization techniques used in mass spectrometry. It discusses gas phase ionization methods like electron impact and chemical impact ionization. It also covers desorptive ionization techniques such as field desorption, fast atom bombardment, and matrix-assisted laser desorption ionization. Finally, it summarizes evaporative ionization methods like atmospheric pressure chemical ionization and atmospheric pressure photoionization. The document aims to explain the basic principles, applications, advantages, and limitations of various ionization methods for mass spectrometry analysis.
The document provides an overview of mass spectrometry, including its basic principles, components, working principle, and various applications. Mass spectrometry involves ionizing chemical compounds and separating the resulting ions based on their mass-to-charge ratio, producing a mass spectrum that can be used to determine the elemental or isotopic composition of a sample. Key components include an ion source, mass analyzer, and detector. Common ionization methods are also described, such as electron impact, chemical ionization, electrospray ionization, and matrix-assisted laser desorption/ionization.
Quadrupole and Time of Flight Mass analysers.Gagangowda58
Description about important mass analysers Quadrupole and TOF: Principle, Construction and Working, Advantages and Disadvantages and their Applications.
Mass spectrometry is an analytical technique that ionizes molecules and separates the resulting ions based on their mass-to-charge ratio. It is a powerful qualitative and quantitative technique used to measure a wide range of clinically relevant analytes. Various ionization sources are used depending on the type of sample, including electron ionization, chemical ionization, electrospray ionization, and matrix-assisted laser desorption/ionization. Ions are accelerated into a mass analyzer such as a quadrupole, magnetic sector, or time-of-flight analyzer which separates the ions based on m/z. The detected ions produce a mass spectrum that provides information about molecular structure.
Mass spectrometry is a technique that ionizes chemical compounds and sorts the ions based on their mass-to-charge ratio. It can be used to determine molecular weights, identify organic and inorganic compounds, and analyze complex mixtures. The key components of a mass spectrometer are an ion source that ionizes samples, a mass analyzer that separates the ions by mass, and a detector that records the results as a mass spectrum. Common applications of mass spectrometry include molecular structure determination, quantitative analysis of mixtures, and identification of unknown compounds.
various parts of mAss spectroscopy, applications, principle, peaks, rules, typical mass spectra, various combinations, Fragmentation, rules of fragmentation and useful points which can help Chemical and analytical students and structural elucidation.
Mass spectrometry and ionization techniquesSurbhi Narang
Mass spectrometry is a technique that identifies chemicals based on their mass and charge. It works by ionizing chemical compounds and separating the resulting ions based on their mass-to-charge ratio. The document discusses the key components and principles of mass spectrometry including various ionization methods, mass analyzers, and applications such as sequencing proteins, determining molecular weights, and drug discovery.
This document provides an introduction to mass spectrometry, including definitions, principles, instrumentation, ionization techniques, applications, advantages, and disadvantages. It describes how mass spectrometry works to ionize chemical compounds and measure their mass-to-charge ratios to determine molecular structures. The key components of a mass spectrometer and various ionization methods are defined. Applications including qualitative analysis, quantitative analysis, proteomics, and combination with chromatography are summarized.
Atmospheric Pressure Chemical IonizationVISHAL THAKUR
Atmospheric Pressure Chemical Ionization
This is an ionization method in which the sample is ionized using an ion – molecule reaction with a reactant ion.
Instrumentation and application of LC-MS/MS in bioanalysisDr. Amit Patel
This document discusses LC-MS/MS instrumentation and applications in bioanalysis. It provides an overview of the principles of mass spectrometry and why MS is needed for bioanalysis. It then describes the components, workflow and applications of LC-MS/MS systems, focusing on their use in quantifying drugs and metabolites in biological samples. A case study on analyzing the drug sulfasalazine by LC-MS/MS is also presented.
This document discusses several ionization techniques used in mass spectrometry including electron impact ionization, chemical ionization, field ionization, MALDI, FAB, ESI, APCI, APPI, and their applications. It also describes the working of common mass analyzers like quadrupole mass analyzer and time-of-flight analyzer. Finally, it mentions some applications of mass spectrometry like protein characterization, isotope tracking, molecular weight determination, studying reaction mechanisms etc.
This slide discusses the principle, instrumentation, process, detectors, sample ,solvents used in mass spectroscopy and also its applications and limitations.
Electrophoresis by Anubhav Singh, M.pharmAnubhav Singh
This document provides an overview of electrophoresis. It begins by explaining how electrophoresis works, noting that when an electric field is applied to a colloidal solution, colloidal particles migrate toward either the positive or negative electrode depending on their charge. It then discusses several types of electrophoresis, including SDS electrophoresis, native gels, electrofocusing gels, and DNA agarose gels. The document also outlines the basic equipment and process for performing electrophoresis, including sample delivery, gel preparation, loading samples, running the gel, and analyzing results. It concludes by mentioning some applications of electrophoresis like DNA sequencing and medical research.
The aim of the coupling is to obtain an information-rich detection for both identification and quantification compared to that with a single analytical technique.
Mass spectrometry(Ionization Techniques) by Ashutosh PankeAshutosh Panke
The document discusses various ionization techniques used in mass spectrometry. It describes several gas phase ionization methods including electron impact ionization, chemical ionization, and field ionization. It also discusses several desorption ionization techniques, notably fast atom bombardment, matrix assisted laser desorption/ionization, electrospray ionization, and surface enhanced laser desorption/ionization. The document provides details on the mechanisms and applications of these various ionization methods. It also categorizes mass analyzers and discusses time-of-flight mass analyzers.
Mass spectrometry basic principle & Instrumentationmanojjeya
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.
Mass spectroscopy
1.Introduction
2. Principle
3. Theory
4. Instrumentation
5. Different types of Ionization
6. FAB
7. MALDI
8. APCI
9. ESI
10.Quardapole
This document discusses mass spectrometry, including its principles, instrumentation, and applications. Mass spectrometry works by ionizing molecules and measuring their mass-to-charge ratios, producing a mass spectrum. This technique is used to determine molecular masses and structures of unknown compounds. It has various applications in analytical chemistry and biology due to its ability to distinguish between substances with high sensitivity and specificity.
Mass Spectrometry Applications and spectral interpretation: BasicsShreekant Deshpande
Mass spectrometry is a powerful analytical tool that is extensively used in fields like biotechnology, pharmaceuticals, clinical research, and environmental analysis. It works by ionizing molecule samples and then separating the ions based on their mass-to-charge ratio, which provides information about molecular structure. This information can be used to identify unknown compounds, study reaction mechanisms, and more. Mass spectrometry requires only picomolar concentrations of samples and can detect small changes in molecular structure. It has various applications in medicinal chemistry, such as determining molecular weights, monitoring chemical reactions, elucidating unknown structures, and identifying drug mechanisms of action.
MALDI-TOF mass spectrometry allows for the analysis of biomolecules like proteins, peptides, and oligonucleotides. It works by co-crystallizing the sample with an absorbing matrix on a target plate. A laser is used to excite the matrix, transferring energy to the analyte and causing it to desorb and ionize. The ionized analyte is then accelerated into a time-of-flight mass analyzer which separates the ions based on their mass-to-charge ratio, allowing for molecular weight determination. This technique is gentle, accurate, and useful for determining post-translational modifications or mutations.
MALDI...
This Presentation Contain following...
#Introduction
#Matrix and examples
#Considerations of Matrix Material
#MALDI Sample Preparation
#Mechanism of MALDI
#Mass Spectrometer
#Reproducibility and Performance
#Uses of MALDI
#Conclusion
#References
Thanks For Help and Guidance of Mr. D.V. Mahuli Sir and Mr. V.T. Pawar Sir
This document provides an overview of different ionization techniques used in mass spectrometry. It discusses gas phase ionization methods like electron impact and chemical impact ionization. It also covers desorptive ionization techniques such as field desorption, fast atom bombardment, and matrix-assisted laser desorption ionization. Finally, it summarizes evaporative ionization methods like atmospheric pressure chemical ionization and atmospheric pressure photoionization. The document aims to explain the basic principles, applications, advantages, and limitations of various ionization methods for mass spectrometry analysis.
The document provides an overview of mass spectrometry, including its basic principles, components, working principle, and various applications. Mass spectrometry involves ionizing chemical compounds and separating the resulting ions based on their mass-to-charge ratio, producing a mass spectrum that can be used to determine the elemental or isotopic composition of a sample. Key components include an ion source, mass analyzer, and detector. Common ionization methods are also described, such as electron impact, chemical ionization, electrospray ionization, and matrix-assisted laser desorption/ionization.
Quadrupole and Time of Flight Mass analysers.Gagangowda58
Description about important mass analysers Quadrupole and TOF: Principle, Construction and Working, Advantages and Disadvantages and their Applications.
Mass spectrometry is an analytical technique that ionizes molecules and separates the resulting ions based on their mass-to-charge ratio. It is a powerful qualitative and quantitative technique used to measure a wide range of clinically relevant analytes. Various ionization sources are used depending on the type of sample, including electron ionization, chemical ionization, electrospray ionization, and matrix-assisted laser desorption/ionization. Ions are accelerated into a mass analyzer such as a quadrupole, magnetic sector, or time-of-flight analyzer which separates the ions based on m/z. The detected ions produce a mass spectrum that provides information about molecular structure.
Mass spectrometry is a technique that ionizes chemical compounds and sorts the ions based on their mass-to-charge ratio. It can be used to determine molecular weights, identify organic and inorganic compounds, and analyze complex mixtures. The key components of a mass spectrometer are an ion source that ionizes samples, a mass analyzer that separates the ions by mass, and a detector that records the results as a mass spectrum. Common applications of mass spectrometry include molecular structure determination, quantitative analysis of mixtures, and identification of unknown compounds.
various parts of mAss spectroscopy, applications, principle, peaks, rules, typical mass spectra, various combinations, Fragmentation, rules of fragmentation and useful points which can help Chemical and analytical students and structural elucidation.
Mass spectrometry and ionization techniquesSurbhi Narang
Mass spectrometry is a technique that identifies chemicals based on their mass and charge. It works by ionizing chemical compounds and separating the resulting ions based on their mass-to-charge ratio. The document discusses the key components and principles of mass spectrometry including various ionization methods, mass analyzers, and applications such as sequencing proteins, determining molecular weights, and drug discovery.
This document provides an introduction to mass spectrometry, including definitions, principles, instrumentation, ionization techniques, applications, advantages, and disadvantages. It describes how mass spectrometry works to ionize chemical compounds and measure their mass-to-charge ratios to determine molecular structures. The key components of a mass spectrometer and various ionization methods are defined. Applications including qualitative analysis, quantitative analysis, proteomics, and combination with chromatography are summarized.
Atmospheric Pressure Chemical IonizationVISHAL THAKUR
Atmospheric Pressure Chemical Ionization
This is an ionization method in which the sample is ionized using an ion – molecule reaction with a reactant ion.
Instrumentation and application of LC-MS/MS in bioanalysisDr. Amit Patel
This document discusses LC-MS/MS instrumentation and applications in bioanalysis. It provides an overview of the principles of mass spectrometry and why MS is needed for bioanalysis. It then describes the components, workflow and applications of LC-MS/MS systems, focusing on their use in quantifying drugs and metabolites in biological samples. A case study on analyzing the drug sulfasalazine by LC-MS/MS is also presented.
This document discusses several ionization techniques used in mass spectrometry including electron impact ionization, chemical ionization, field ionization, MALDI, FAB, ESI, APCI, APPI, and their applications. It also describes the working of common mass analyzers like quadrupole mass analyzer and time-of-flight analyzer. Finally, it mentions some applications of mass spectrometry like protein characterization, isotope tracking, molecular weight determination, studying reaction mechanisms etc.
This slide discusses the principle, instrumentation, process, detectors, sample ,solvents used in mass spectroscopy and also its applications and limitations.
Electrophoresis by Anubhav Singh, M.pharmAnubhav Singh
This document provides an overview of electrophoresis. It begins by explaining how electrophoresis works, noting that when an electric field is applied to a colloidal solution, colloidal particles migrate toward either the positive or negative electrode depending on their charge. It then discusses several types of electrophoresis, including SDS electrophoresis, native gels, electrofocusing gels, and DNA agarose gels. The document also outlines the basic equipment and process for performing electrophoresis, including sample delivery, gel preparation, loading samples, running the gel, and analyzing results. It concludes by mentioning some applications of electrophoresis like DNA sequencing and medical research.
The aim of the coupling is to obtain an information-rich detection for both identification and quantification compared to that with a single analytical technique.
Mass spectrometry(Ionization Techniques) by Ashutosh PankeAshutosh Panke
The document discusses various ionization techniques used in mass spectrometry. It describes several gas phase ionization methods including electron impact ionization, chemical ionization, and field ionization. It also discusses several desorption ionization techniques, notably fast atom bombardment, matrix assisted laser desorption/ionization, electrospray ionization, and surface enhanced laser desorption/ionization. The document provides details on the mechanisms and applications of these various ionization methods. It also categorizes mass analyzers and discusses time-of-flight mass analyzers.
Mass spectrometry basic principle & Instrumentationmanojjeya
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.
Mass spectroscopy
1.Introduction
2. Principle
3. Theory
4. Instrumentation
5. Different types of Ionization
6. FAB
7. MALDI
8. APCI
9. ESI
10.Quardapole
This document discusses mass spectrometry, including its principles, instrumentation, and applications. Mass spectrometry works by ionizing molecules and measuring their mass-to-charge ratios, producing a mass spectrum. This technique is used to determine molecular masses and structures of unknown compounds. It has various applications in analytical chemistry and biology due to its ability to distinguish between substances with high sensitivity and specificity.
Mass Spectrometry Applications and spectral interpretation: BasicsShreekant Deshpande
Mass spectrometry is a powerful analytical tool that is extensively used in fields like biotechnology, pharmaceuticals, clinical research, and environmental analysis. It works by ionizing molecule samples and then separating the ions based on their mass-to-charge ratio, which provides information about molecular structure. This information can be used to identify unknown compounds, study reaction mechanisms, and more. Mass spectrometry requires only picomolar concentrations of samples and can detect small changes in molecular structure. It has various applications in medicinal chemistry, such as determining molecular weights, monitoring chemical reactions, elucidating unknown structures, and identifying drug mechanisms of action.
MALDI-TOF mass spectrometry allows for the analysis of biomolecules like proteins, peptides, and oligonucleotides. It works by co-crystallizing the sample with an absorbing matrix on a target plate. A laser is used to excite the matrix, transferring energy to the analyte and causing it to desorb and ionize. The ionized analyte is then accelerated into a time-of-flight mass analyzer which separates the ions based on their mass-to-charge ratio, allowing for molecular weight determination. This technique is gentle, accurate, and useful for determining post-translational modifications or mutations.
MALDI-TOF: Pricinple and Its Application in Biochemistry and BiotechnologyDevakumar Jain
The document discusses MALDI-TOF (matrix-assisted laser desorption/ionization time-of-flight) mass spectrometry. It provides a history of the development of mass spectrometry techniques. MALDI-TOF allows for the analysis of intact biomolecules like proteins and is a soft ionization method. It provides high sensitivity and mass accuracy for analyzing proteins, peptides, and other large biomolecules. The document also discusses applications of MALDI-TOF like protein identification and characterization.
Part of of a series of technical seminars held at my institute. My presentation focused on the use of mass spectrometry in the analysis of biological samples.
This document provides an overview of polymer analysis using mass spectrometry. It discusses what mass spectrometry is and the types of information it can provide about molecular mass and structure. It also describes how mass spectrometers work by introducing samples, ionizing them, analyzing the ions, and detecting them. Specific ionization methods like electrospray ionization and applications of mass spectrometry in areas like biotechnology and pharmaceuticals are summarized. The document concludes by outlining how mass spectrometry is used for polymer analysis by providing detailed structural and compositional information.
Mass spectrometry is an analytical technique that identifies unknown compounds and quantifies known materials by measuring their mass-to-charge ratios. It works by ionizing chemical compounds, generating charged molecule fragments, and measuring their mass-to-charge ratios using techniques like time-of-flight analysis. The document discusses the principles, instrumentation including ion sources, mass analyzers, and detectors, applications in fields like proteomics and metabolomics, and guidelines for interpreting mass spectra.
Mass spectrometry is an analytical technique that measures the molecular mass of samples. It provides accurate molecular weight measurements and can generate structural information by fragmenting samples. Mass spectrometers are used in various fields including biotechnology, pharmaceuticals, clinical analysis, environmental analysis, and geology. They work by ionizing samples, separating the ions by mass-to-charge ratio using an analyzer, and detecting the ions. Common ionization methods for biochemical analysis include electrospray ionization and matrix-assisted laser desorption ionization.
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.
Mass spectroscopy is an analytical technique used to measure the mass-to-charge ratio (m/z) of one or more molecules present in a sample. It can be used to identify unknown compounds via molecular weight determination, quantify known compounds, and determine the structure and chemical properties of molecules.2 Mass spectroscopy is also useful for studies on protein-protein interactions. The basic principle involves fragmentation of a compound or molecule into charged species, which are accelerated, deflected, and finally focused on a detector according to their mass and charge ratio.Mass spectroscopy is an instrumental method for identifying the chemical constitution of a substance by means of the separation of gaseous ions according to their differing mass and charge.
i. The fragment I can identify is C3H7+ with m/z 57.
ii. The molecular ion is M+ with m/z 88, indicating the molecular formula is C6H14O. The functional groups are alcohol (-OH) and alkyl groups (-CH3, -CH2-).
iii. Expected fragmentation processes:
- Loss of H2O (18 Da) to form M+ - 18
- Loss of CH3 (15 Da) to form M+ - 15
- Loss of C2H5 (29 Da) to form M+ - 29
iv. The peaks at m/z 57, 71 and 73 correspond to the fragments C3H7+, M
Presentation on the basic Maldi-Imaging workflow with some information on how...Diane Hatziioanou
Presentation on the basic Maldi-Imaging workflow with some information on how it works. This presentation was prepared for a group meeting and is focused almost entirely on the process of MALDI-Imaging to give the group leaders an understanding of the process as well as some important information on how to make it work well.
This document discusses mass spectrometry and provides information on several related topics:
- Mass spectrometry involves ionizing molecules and analyzing the resulting ions based on their mass-to-charge ratios to obtain molecular fingerprints.
- Different ionization methods like electron ionization, chemical ionization, electrospray ionization, and matrix-assisted laser desorption/ionization are described.
- Mass analyzers including quadrupoles and time-of-flight instruments are discussed. Factors like resolution, mass accuracy, calibration, adduct formation, and fragmentation are also covered.
Liquid chromatography–mass spectrometry (LC-MS) combines liquid chromatography and mass spectrometry to separate and analyze compounds. It works by separating compounds using liquid chromatography and then analyzing the separated molecular ions and fragments using mass spectrometry. This allows LC-MS to identify unknown compounds and determine their molecular weight. LC-MS is useful for applications like drug development, molecular structure determination, and metabolite identification due to its high sensitivity and selectivity.
Methodology of targeted mass spectrometryMoustafa Rezk
This document discusses targeted mass spectrometry methodology. It describes how mass spectrometry can be used with gas chromatography (GC) or liquid chromatography (LC) for definitive identification of samples. Mass spectrometry provides specificity, selectivity, sensitivity and speed for analysis. Common applications include pharmaceutical analysis, forensics, food testing and environmental analysis. The document outlines the basic components and processes of mass spectrometry, including sample introduction, ionization techniques like electron ionization and electrospray ionization, mass analyzers like quadrupoles and ion traps, and tandem mass spectrometry.
The document discusses liquid chromatography-mass spectrometry (LC-MS), a hyphenated technique that combines liquid chromatography with mass spectrometry. It describes the basic components and workings of LC, MS, and LC-MS. Key interfaces for LC-MS coupling include electrospray ionization, atmospheric pressure chemical ionization, and atmospheric pressure photoionization. Common mass analyzers are quadrupoles, ion traps, and time-of-flight analyzers. The document outlines applications of LC-MS such as drug discovery, food analysis, and environmental and biomedical studies.
The document provides information about mass spectrometry including:
- Mass spectrometry is a powerful analytical technique that uses instruments called mass spectrometers to identify molecules by breaking them into ionized fragments and measuring their mass-to-charge ratios.
- The basic components of a mass spectrometer are the sample inlet, ionization source, mass analyzer, and ion detector. Common ionization sources are electrospray ionization, matrix-assisted laser desorption/ionization, and electron ionization. Common mass analyzers are quadrupoles, ion traps, and time-of-flight.
- Mass spectrometry has a variety of applications and has undergone significant technological developments since its invention in the early 20th
This document discusses mass spectrometry and its applications in proteomics. It describes how mass spectrometry works by ionizing molecules and measuring their mass-to-charge ratios. Key developments in the technology are outlined, including the introduction of soft ionization techniques like MALDI and ESI that enabled the analysis of proteins. The document discusses various mass analyzers and how tandem mass spectrometry is used to obtain structural information through fragmentation. Applications of mass spectrometry in proteomics include protein identification, characterization of post-translational modifications, and quality control of recombinant proteins.
This document summarizes research using a radio frequency sensor to detect and distinguish particle concentration. The RF sensor uses changes in dielectric permittivity to detect particles without labelling. Test results showed the sensor could detect 4 μm polystyrene particles at different concentrations and frequencies, and distinguish between 1% and 10% concentrations. Future work will further test the sensor's ability to detect different particles and concentrations at more frequencies to support its use in applications like medicine, biology and environmental monitoring.
Proteins are composed of amino acids linked together through peptide bonds. Peptides are short chains of amino acids, while proteins can be made of long chains of amino acids folded into shapes. Proteins can be classified based on their size and shape as globular or fibrous proteins, or based on their functions such as structural, regulatory, catalytic, transport, genetic, storage and defense proteins. Some peptides act as toxins or have important roles as hormones, antibiotics, or in oxidation reduction systems.
The document discusses the four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids in the peptide chain. The secondary structure involves hydrogen bonding that causes the chain to fold into structures like alpha helices or beta sheets. Tertiary structure describes further folding and interactions that result in the protein's three-dimensional shape. Quaternary structure refers to multiple peptide chains linked together in a protein.
Lipoproteins are spherical complexes formed by lipids and proteins that transport insoluble lipids through the blood. There are four main classes of lipoproteins: chylomicrons, very low density lipoproteins (VLDL), low density lipoproteins (LDL), and high density lipoproteins (HDL). Chylomicrons and VLDL are involved in transporting triglycerides, LDL transports cholesterol, and HDL transports excess cholesterol from tissues back to the liver.
This document provides information about lipids and fatty acids. It begins with an outline of chapter topics on the chemistry and classification of lipids. It then defines lipids and lists their main functions in the body. Lipids are classified as simple, complex, or derived, and as saponifiable or non-saponifiable. Key reactions for lipids include hydrolysis. Fatty acids are classified based on saturation and chain length. Essential fatty acids, which must be obtained through diet, are discussed. Neutral fats are described as triacylglycerols composed of glycerol and fatty acids.
This document discusses lipids and fatty acids. It defines lipids and lists their main functions. Lipids are classified as simple, complex, or derived, and as saponifiable or non-saponifiable. Fatty acids are described, including their chemistry, classification as saturated or unsaturated, nomenclature, and examples of biologically important fatty acids. Essential fatty acids are discussed along with their importance.
This document summarizes the digestion, absorption, and transport of dietary lipids in the human body. Dietary lipids undergo limited digestion in the mouth and stomach by lipases before entering the intestine, where pancreatic enzymes emulsify and break down triglycerides, phospholipids, and cholesterol esters into absorbable components. These components are absorbed via micelle transport into intestinal cells and repackaged into chylomicrons that enter the bloodstream. Chylomicrons deliver lipids to tissues and lose triglycerides due to lipoprotein lipase activity before remnants are removed from circulation by the liver.
This document provides information about lipids and fatty acids. It begins by defining lipids and listing their main functions in the body. It then classifies lipids as simple, complex, or derived, and as saponifiable or non-saponifiable. The document further describes the chemistry and classification of fatty acids, including saturated, unsaturated, monounsaturated, and polyunsaturated fatty acids. It also discusses the nomenclature and isomerism of fatty acids. The key reactions of triacylglycerols are described.
Hormones are chemical messengers that are secreted into the blood by endocrine glands and have profound effects on metabolic processes and cellular communication. They can be classified based on their chemical composition, location of receptors, or solubility. The major classes of hormones include steroids such as sex and adrenal hormones, peptides/proteins such as insulin and growth hormone, and amines such as epinephrine. Steroid hormones are derived from cholesterol and include estrogens, androgens, progesterone, corticosteroids, and aldosterone. Peptide hormones include insulin, glucagon, and somatostatin which are secreted by the pancreas, as well as hormones from the pituitary, parathyroid,
This document discusses enzymes and their properties. It begins by defining enzymes as globular proteins that act as biological catalysts to facilitate chemical reactions in living organisms. It then describes general enzyme characteristics such as their catalytic power, specificity, and ability to have their activity regulated. The document discusses how enzymes are named using systematic and common nomenclature systems. It also covers enzyme classification, cofactors/coenzymes, mechanisms of action, factors that influence activity, and kinetic models like Michaelis-Menten. Overall, the document provides a comprehensive overview of the key concepts regarding enzymes.
1. The urea cycle is a series of enzymatic reactions that occurs primarily in the liver to convert toxic ammonia produced from amino acid catabolism into urea for excretion.
2. The cycle involves five principal reactions: carbamoyl phosphate synthesis, citrulline synthesis, argininosuccinate synthesis, argininosuccinate cleavage, and arginine cleavage into ornithine and urea.
3. The urea cycle serves two major biological roles - detoxification of ammonia into urea and biosynthesis of the amino acid arginine from ornithine in tissues like liver, kidney, and intestine.
1) Fatty acids undergo beta-oxidation in the mitochondria to break them down into acetyl-CoA units, releasing energy.
2) Beta-oxidation involves a four-step cycle that removes two-carbon acetyl-CoA units from the fatty acid.
3) The complete breakdown of a fatty acid like stearic acid yields 9 acetyl-CoA molecules which enter the citric acid cycle, producing a total of 146 ATP molecules through electron transport chain reactions.
Glycogen metabolism involves the breakdown of glycogen to glucose-6-phosphate through glycogenolysis. Glycogenolysis occurs in three steps: 1) glycogen phosphorylase cleaves glucose from glycogen, 2) transferase and alpha-1,6-glucosidase remodel glycogen to allow further degradation, and 3) phosphoglucomutase converts glucose-1-phosphate to glucose-6-phosphate. In liver, glucose-6-phosphatase converts glucose-6-phosphate to glucose for blood glucose regulation. In muscle, glucose-6-phosphate enters glycolysis for rapid energy production.
This document discusses glycogen metabolism. It notes that glycogen is a readily available form of glucose storage found primarily in the liver and muscles. Glycogen synthesis, or glycogenesis, occurs in the fed state in these tissues and involves three steps - isomerization of glucose-6-phosphate to glucose-1-phosphate, activation of glucose-1-phosphate to UDP-glucose, and linkage of UDP-glucose to a glycogen chain catalyzed by glycogen synthase. Glycogen branching is accomplished by the enzyme amylo-(1,4-1,6)-trans-glycosylase which transfers glycogen segments to form branches. The synthesis and breakdown of glycogen in the liver and muscles
Gluconeogenesis is the metabolic pathway by which glucose is synthesized from non-carbohydrate materials to maintain blood glucose levels during periods without food intake. It takes place primarily in the liver and involves bypasses of three irreversible steps in glycolysis. Precursors like lactate, glycerol, and certain amino acids are converted to pyruvate and then glucose. The pathway requires energy in the form of 6 ATP molecules to synthesize one glucose molecule from two pyruvate. Gluconeogenesis is important for supplying glucose to tissues like the brain and helps maintain normal blood sugar through processes like the Cori cycle.
The citric acid cycle is the principal process for generating reduced coenzymes NADH and FADH2, which are necessary for ATP synthesis. It takes place in the mitochondrial matrix and involves eight steps catalyzed by different enzymes. Acetyl-CoA enters the cycle and is oxidized, producing carbon dioxide and the reduced coenzymes that fuel ATP production. Regulation occurs at three steps to precisely adjust the cycle's rate according to cellular energy needs. Overall, 12 ATP molecules are generated for each acetyl-CoA molecule that completes the citric acid cycle.
This document provides an overview of cholesterol biosynthesis, which occurs in most cells but primarily in the liver and intestine. There are 5 stages: 1) acetyl-CoA is converted to mevalonate, 2) mevalonate is converted to activated isoprene units, 3) six isoprene units condense to form squalene, 4) squalene is cyclized to lanosterol, and 5) lanosterol is converted to cholesterol over 20 steps. HMG-CoA reductase, which converts HMG-CoA to mevalonate, is the rate-limiting step and is regulated by feedback from cholesterol and bile acids as well as hormones like insulin, glucagon
This document provides information on carbohydrates and monosaccharides. It defines carbohydrates and explains their four main functions in living organisms. It then classifies carbohydrates into monosaccharides, disaccharides, oligosaccharides, and polysaccharides. The document focuses on monosaccharides, describing their structures, classifications, stereochemistry including D and L isomers, anomers, mutarotation, and important naturally occurring monosaccharides like glucose, fructose, and ribose. It also outlines important reactions of monosaccharides such as oxidation, reduction, glycoside formation, and phosphate ester formation.
This document provides an overview of carbohydrate biochemistry. It defines carbohydrates as polyhydroxy aldehydes or ketones and classifies them based on molecular size into monosaccharides, disaccharides, oligosaccharides, and polysaccharides. Monosaccharides are further classified as aldoses or ketoses depending on whether they have an aldehyde or ketone functional group. The document discusses carbohydrate stereochemistry, including D and L isomers, enantiomers, and diastereomers. It also covers optical activity and how carbohydrate enantiomers can rotate plane-polarized light. Epimers are described as diastereomers that differ at only one chiral carbon.
This document summarizes the processes of transcription and translation. It explains that during transcription, RNA polymerase makes an mRNA copy of a gene from DNA. The mRNA then moves to the ribosomes in the rough ER for translation. During translation, ribosomes and tRNA molecules work together to translate the mRNA into a polypeptide chain according to the mRNA's codon sequence. The process continues until a stop codon is reached, and the polypeptide chain is released. Mutations can occur during these processes, potentially resulting in non-functional or disease-causing proteins. Examples of different mutation types and their effects are provided.
Nucleic acids are macromolecules made of nucleotides that contain three components: a 5-carbon sugar, phosphate group, and nitrogenous base. DNA and RNA are the two main types of nucleic acids. DNA contains the sugar deoxyribose and has a double helix structure, while RNA contains the sugar ribose and is single-stranded. Both are composed of nucleotides joined by phosphodiester bonds and function to carry genetic information for protein synthesis. Their primary differences are that DNA contains the base thymine while RNA contains uracil, and RNA is found in the cytoplasm while DNA remains in the nucleus.
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1. Mass Spectrometry 101
An Introductory Lecture On Mass Spectrometry
Fundamentals
Presented to the Sandler Mass Spectrometry Users’ Group
University of California San Francisco
April 11, 2003
2. What does a mass spectrometer do?
1. It measures mass better than any other technique.
2. It can give information about chemical structures.
What are mass measurements good for?
To identify, verify, and quantitate: metabolites,
recombinant proteins, proteins isolated from natural
sources, oligonucleotides, drug candidates, peptides,
synthetic organic chemicals, polymers
3. Pharmaceutical analysis
Bioavailability studies
Drug metabolism studies, pharmacokinetics
Characterization of potential drugs
Drug degradation product analysis
Screening of drug candidates
Identifying drug targets
Biomolecule characterization
Proteins and peptides
Oligonucleotides
Environmental analysis
Pesticides on foods
Soil and groundwater contamination
Forensic analysis/clinical
Applications of Mass Spectrometry
4. How does a mass spectrometer work?
Ion source:
makes ions
Mass
analyzer:
separates
ions
Mass spectrum:
presents
information
Sample
12. ¤ Operate under high vacuum (keeps ions from bumping
into gas molecules)
¤ Actually measure mass-to-charge ratio of ions (m/z)
¤ Key specifications are resolution, mass measurement
accuracy, and sensitivity.
¤ Several kinds exist: for bioanalysis, quadrupole, time-of-
flight and ion traps are most used.
Mass analyzers separate ions based on their
mass-to-charge ratio (m/z)
13. Quadrupole Mass Analyzer
Uses a combination of RF
and DC voltages to operate
as a mass filter.
• Has four parallel metal
rods.
• Lets one mass pass
through at a time.
• Can scan through all
masses or sit at one
fixed mass.
14. mass scanning mode
m1m3m4 m2
m3
m1
m4
m2
single mass transmission mode
m2 m2 m2 m2
m3
m1
m4
m2
Quadrupoles have variable ion transmission modes
15. Time-of-flight (TOF) Mass Analyzer
+
+
+
+
Source Drift region (flight tube)
detector
V
• Ions are formed in pulses.
• The drift region is field free.
• Measures the time for ions to reach the detector.
• Small ions reach the detector before large ones.
20. The mass spectrum shows the results
RelativeAbundance
Mass (m/z)
0
10000
20000
30000
40000
50000 100000 150000 200000
MH+
(M+2H)2+
(M+3H)3+
MALDI TOF spectrum of IgG
21. ESI Spectrum of Trypsinogen (MW 23983)
1599.8
1499.9
1714.1
1845.9
1411.9
1999.6
2181.6
M + 15 H+
M + 13 H+
M + 14 H+
M + 16 H+
m/z Mass-to-charge ratio
22. How do mass spectrometers get their names?
Types of ion sources:
• Electrospray (ESI)
• Matrix Assisted Laser Desorption Ionization (MALDI)
Types of mass analyzers:
• Quadrupole (Quad, Q)
• Ion Trap
• Time-of-Flight (TOF)
-Either source type can work with either analyzer type: “MALDI-
TOF,” “ESI-Quad.”
-Analyzers can be combined to create “hybrid” instruments.
ESI-QQQ, MALDI QQ TOF, Q Trap
23. Voyager-DE STR MALDI TOF
Camera
Laser
Sample
plate
Pumping Pumping
Timed ion
selector Reflector
Linear
detector
Extraction
grids
Reflector
detector
24. QSTARTM
ESI QQ TOF or MALDI QQ TOF
Q1
Ion Mirror
(reflector)
Effective Flight
Path = 2.5 m
Q2
Q0
Sample
25. QTRAP: Linear Ion Trap on a Triple Quadrupole
A new type of instrument….
linear ion trap
Exit
Q0 Q1 Q2 Q3
26. Inlet
Ionization
Mass Analyzer
Mass Sorting (filtering)
Ion
Detector
Detection
Ion
Source
• Solid
• Liquid
• Vapor
Detect ions
Form ions
(charged molecules)
Sort Ions by Mass (m/z)
1330 1340 1350
100
75
50
25
0
Mass Spectrum
Summary: acquiring a mass spectrum
27. Assigning numerical value to the intrinsic property
of “mass” is based on using carbon-12, 12C, as a
reference point.
One unit of mass is defined as a Dalton (Da).
One Dalton is defined as 1/12 the mass of a single
carbon-12 atom.
Thus, one 12C atom has a mass of 12.0000 Da.
How is mass defined?
28. Isotopes
+Most elements have more than one stable isotope.
For example, most carbon atoms have a mass of 12 Da, but in
nature, 1.1% of C atoms have an extra neutron, making their mass
13 Da.
+Why do we care?
Mass spectrometers can “see” isotope peaks if their resolution is
high enough.
If an MS instrument has resolution high enough to resolve these
isotopes, better mass accuracy is achieved.
29. Element Mass Abundance
H 1.0078
2.0141
99.985%
0.015
C 12.0000
13.0034
98.89
1.11
N 14.0031
15.0001
99.64
0.36
O 15.9949
16.9991
17.9992
99.76
0.04
0.20
Stable isotopes of most abundant elements of
peptides
32. Mass spectrum of insulin
12C : 5730.61
13C
2 x 13C
Insulin has 257 C-atoms. Above this mass, the monoisotopic
peak is too small to be very useful, and the average mass is
usually used.
34. Average mass
Average mass corresponds
to the centroid of the
unresolved peak cluster
When the isotopes are not resolved, the centroid of the envelope
corresponds to the weighted average of all the the isotope peaks in
the cluster, which is the same as the average or chemical mass.
35. 6130 6140 6150 6160 6170
Poorer
resolution
Better
resolution
What if the resolution is not so good?
At lower resolution, the mass measured is the average mass.
Mass
36. 15.01500 15.01820 15.02140 15.02460 15.02780 15.03100
Mass(m/z)
100
0
10
20
30
40
50
60
70
80
90
100
%Intensity
ISO:CH3
15.0229
M
FWHM = DM
R = M/DM
How is mass resolution calculated?
37. Mass measurement accuracy depends on resolution
0
2000
4000
6000
8000
Counts
2840 2845 2850 2855
Mass (m/z)
Resolution = 14200
Resolution = 4500
Resolution =18100
15 ppm error
24 ppm error
55 ppm error
High resolution means better mass accuracy
38. How do we achieve superior mass
resolution?
Delayed Extraction on a MALDI source
Reflector TOF Mass Analyzer
39. Important performance factors
Mass accuracy: How accurate is the mass
measurement?
Resolution: How well separated are the peaks
from each other?
Sensitivity: How small an amount can be
analyzed?
40. What is MSMS?
MS/MS means using two mass analyzers (combined
in one instrument) to select an analyte (ion) from a
mixture, then generate fragments from it to give
structural information.
Ion
source
MS-2MS-1
Mixture of
ions
Single
ion
Fragments
41. What is MS/MS?
MS/MS
+
+
+ +
+
1 peptide
selected for
MS/MS
The masses of all
the pieces give an
MS/MS spectrum
Peptide
mixture
Have only masses
to start
42. Interpretation of an MSMS spectrum to derive
structural information is analogous to solving
a puzzle
+
+
+ +
+
Use the fragment ion masses as specific pieces of
the puzzle to help piece the intact molecule back
together
44. E G S F F G E E N P N V A R
Peptide Fragmentation
175.10
246.14
345.21
459.25
556.30
670.35
799.39
928.43
985.45
1132.52
1279.59
1366.62
1423.64
1552.69
=>
=
=
=
E=Glu
G=Gly
S=Ser
F=Phe
N=Asn
P=Pro
V=Val
A=Ala
R=Arg
45. Protein Identification
1. Peptide Mass Finger Printing (PMF)
from MS data
2. Database search using fragment ion masses
from MS/MS data
3. Sequence Tags
from MS/MS data
47. Mass Spectrometrist
1. Interview biologist who
isolated the protein
2. Cleave protein to obtain
peptide mixture
3. Analyze peptide mixture by
MS to obtain peptide
molecular masses!
GATHER EVIDENCE
Police Officer
1. Interview witnesses
2. Dust for fingerprints
enzyme
48. DATABASE SEARCH
Police Officer
Height: 5’7”
Weight: 160 lbs
Gender: male
Age: 35-40
Fingerprints
Mass Spectrometrist
Approx. molecular weight: 30,000
Origin: bovine liver
Peptide mass list from MS analysis:
975.4832, 1112.5368, 632.3147,
803.4134, 764.3892
DATABASE OF
KNOWN FELONS
PEPTIDE MASS
DATABASE
OF KNOWN
PROTEINS
search search
49. DATABASE SEARCH RESULTS
Police Officer
Identifies the robber
Anthony J. Felon
Mass Spectrometrist
Identifies the protein
bovine carbonic anhydrase
54. 500 610 720 830 940 1050
Mass(m/z)
0
6735.5
0
10
20
30
40
50
60
70
80
90
100
%Intensity
StitchedPSD=>BC=>SM25=>AdvBC(32,0.5,0.1)[BP=120.1,50520]
y4(+1)
b5(+1)
y8(+1)
y4-17(+1)
a5(+1)
647.4
714.8
y7(+1)
AFQLFD(+1)-17,AFQLFD(+1)-18
730.1
973.7
961.0
819.9
941.5
b7(+1)
65 152 239 326 413 500
Mass(m/z)
0
5.1E+4
0
10
20
30
40
50
60
70
80
90
100
%Intensity
StitchedPSD=>BC=>SM25=>AdvBC(32,0.5,0.1)[BP=120.1,50520]F
y1(+1)
b2(+1)
FQ(+1)
Q
a2(+1)
b4(+1),QLFD(+1)-28
L
b1-18(+1)
165.1
365.1
347.1
y2(+1)
y3-17(+1)
QL(+1)-28
y1-17(+1)
70.0
y3(+1)
84.0
QL(+1)
b3-18(+1),AFQ(+1)-17
229.2
FQL(+1),QLF(+1)
FD(+1)
b4-18(+1)
MS/MS spectrum for tryptic peptide MH+ = 1025.5, EAFQLFDR, from
Spot A. An MS-Tag search using the fragment ions from this spectrum
confirmed the identity of Spot A as myosin light chain.
55. Sequence Tags from Peptide
Fragmentation by MS/MS
peptide molecular weight (MW)
partial sequence (region 2)
molecular wt before partial sequence (region 1)
molecular wts after partial sequence (region 3)
A V I/L T
Peptide measured molecular wt = 1927.2
1108.13Partial Sequence
- A-V-I/L-T-
381.1
region 1 region 2 region 3
One sequence tag includes four components:
1546.11
56. Sequence TAG Example from MS/MS Spectrum
Peptide MW = 1345.70
y 1 1
y 1 0
y 9
y 8
y 7
y 6
y 5
y 4
y 3
y 2
y 1
b1 b2 b3 b4 b5
I/ L
a2
2 9 4 .2
b2 - H2 O
b3 - H2 O
b4 - H2 O
b5 - H2 O
b6 - H2 O
b5 - 2 ( H2 O)
200 400 600 800 1000 1200
m/z, amu
100
200
300
400
500
600
700
800
Sequence Tag (739.34)SVS(I/L)(1120.60)
739.34
1120.60
[M+2H]2+
S V I/LS
58. Acknowledgements
We thank the Applied Biosystems Mass Spectrometry Applications
Laboratory for allowing the use of some of their slides for this
presentation.