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Mass Spectrometry MS
 
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An education video on Mass Spectrometry using a magnetic sector instrument from the Royal Society of Chemistry. From the Modern Instrumental Techniques for schools and colleges DVD. For more information on the Chemistry for our Future programme please visit http://www.rsc.org/CFOF (C) Royal Society of Chemistry
Finding the molecular formula from a mass spectrum
 
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This is the first in a series of 3 lessons about the interpretation of electron impact mass spectra. This video was created for a university course in instrumental analysis in chemistry. Spectra were taken from http://webbook.nist.gov/chemistry/ and used with permission. The isotope calculator mentioned in the video can be found at http://www.sisweb.com/mstools/isotope.htm
Views: 124456 Gary Mabbott
How2: Interpret a mass spectrum
 
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Shows you how to get the information out of a mass spectrum and use it to help suggest the identity of an unidentified molecule
Views: 252444 Andrew Crookell
Mass spectrometry part 1 : introduction
 
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For more information, log on to- http://shomusbiology.com/ Download the study materials here- http://shomusbiology.weebly.com/bio-materials.html Mass spectrometry (MS) is an analytical technique that produces spectra (singular spectrum) of the masses of the molecules comprising a sample of material. The spectra are used to determine the elemental composition of a sample, the masses of particles and of molecules, and to elucidate the chemical structures of molecules, such as peptides and other chemical compounds. Mass spectrometry works by ionizing chemical compounds to generate charged molecules or molecule fragments and measuring their mass-to-charge ratios.[1] In a typical MS procedure, a sample, which may be solid, liquid, or gas, is ionized. The ions are separated according to their mass-to-charge ratio.[1] The ions are detected by a mechanism capable of detecting charged particles. Signal processing results are displayed as spectra of the relative abundance of ions as a function of the mass-to-charge ratio. The atoms or molecules can be identified by correlating known masses to the identified masses or through a characteristic fragmentation pattern. A mass spectrometer consists of three components: an ion source, a mass analyzer, and a detector.[2] The ionizer converts a portion of the sample into ions. There is a wide variety of ionization techniques, depending on the phase (solid, liquid, gas) of the sample and the efficiency of various ionization mechanisms for the unknown species. An extraction system removes ions from the sample, which are then trajected through the mass analyzer and onto the detector. The differences in masses of the fragments allows the mass analyzer to sort the ions by their mass-to-charge ratio. The detector measures the value of an indicator quantity and thus provides data for calculating the abundances of each ion present. Some detectors also give spatial information, e.g. a multichannel plate. Mass spectrometry has both qualitative and quantitative uses. These include identifying unknown compounds, determining the isotopic composition of elements in a molecule, and determining the structure of a compound by observing its fragmentation. Other uses include quantifying the amount of a compound in a sample or studying the fundamentals of gas phase ion chemistry (the chemistry of ions and neutrals in a vacuum). MS is now in very common use in analytical laboratories that study physical, chemical, or biological properties of a great variety of compounds. As an analytical technique it possesses distinct advantages such as: 1. Increased sensitivity over most other analytical techniques because the analyzer, as a mass-charge filter, reduces background interference 2. Excellent specificity from characteristic fragmentation patterns to identify unknowns or confirm the presence of suspected compounds. 3. Information about molecular weight. 4. Information about the isotopic abundance of elements. 5. Temporally resolved chemical data. A few of the disadvantages of the method is that often fails to distinguish between optical and geometrical isomers and the positions of substituent in o-, m- and p- positions in an aromatic ring. Also, its scope is limited in identifying hydrocarbons that produce similar fragmented ions.[3] Source of the article published in description is Wikipedia. I am sharing their material. Copyright by original content developers of Wikipedia. Link- http://en.wikipedia.org/wiki/Main_Page
Views: 203974 Shomu's Biology
Simple explanation of the Mass Spectrometer.
 
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Highly Recommended - Top Tutors for All Subjects at All Levels here: https://spires.co/franklychemistry This short flash animation video outlines the basic principles of a Mass Spectrometer. The key points illustrated are: TINY AMOUNTS OF SAMPLE ARE REQUIRED - THE SAMPLE MUST BE CHANGED TO A VAPOUR - ONE OR MORE ELECTRONS ARE REMOVED FROM ATOMS OR MOLECULES TO PRODUCE +VE IONS - AN ION-ACCELERATING ELECTRIC FIELD, TOGETHER WITH PLATES WITH SLITS, FORMS A NARROW BEAM - A MAGNETIC FIELD DEFLECTS THE ION BEAM - THE ION WITH THE GREATEST MASS AND SMALLEST CHARGE (1+) IS DEFLECTED THE LEAST - IONS HIT A DETECTION PLATE PRODUCING A TINY ELECTRICAL CURRENT THAT IS APPLIFIED - THE MORE IONS OF A SPECIFIC MASS:CHARGE RATIO THE GREATER THE CURRENT AND TALLER THE PEAK
Views: 319410 FranklyChemistry
Mass Spectrometry
 
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009 - Mass Spectrometry In this video Paul Andersen explains how a spectrometer was used to identify the presence of isotopes. This modified Dalton's original atomic theory because atoms of the same element had different masses. The functional parts of a mass spectrometer are detailed including the ionizer, mass analyzer and the detector. A simulation of Chlorine isotopes along with an average atomic mass calculation is included. Music Attribution Title: String Theory Artist: Herman Jolly http://sunsetvalley.bandcamp.com/track/string-theory All of the images are licensed under creative commons and public domain licensing: "File:John Dalton by Charles Turner.jpg." Wikipedia, the Free Encyclopedia. Accessed August 2, 2013. http://en.wikipedia.org/wiki/File:John_Dalton_by_Charles_Turner.jpg. "File:Myoglobin.png." Wikipedia, the Free Encyclopedia. Accessed August 5, 2013. https://en.wikipedia.org/wiki/File:Myoglobin.png. "File:Peptide-Figure-Revised.png." Wikipedia, the Free Encyclopedia. Accessed August 5, 2013. https://en.wikipedia.org/wiki/File:Peptide-Figure-Revised.png. File:WidmoMS.gif, n.d. http://commons.wikimedia.org/wiki/File:WidmoMS.gif.
Views: 232071 Bozeman Science
SamplePrepforMassSpectrometry.wmv
 
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Tips for preparing protein samples from SDS-polyacrylamide gels for mass spectrometry. The processing of a protein sample by Proteomics core facility of Shared Resources, Fred Hutchinson Cancer Research Center is described as well.
Views: 3031 FHCRCSharedResources
Mass Spectrometry Analysis | Mass Spectrometer | Chemistry Notes Class 11| in URDU/HINDI |
 
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Mass Spectrometry Analysis | Mass Spectrometr | Chemistry Notes Class 11| in URDU/HINDI | Mass Spectrometer: Mass spectrometer is an instrument which is used to measure the exact massesof different isotopes of an element. Mass Spectrometery: Which technique is used in this process is called Mass Spectrometery. Firest of all ,Aston's mass spectrograph was designed to identify the isotopes of an element on basis of thier atomic masses.There is an another instrument Called Dempster's mass spectrometer. Analiysis: The substance whose analysis for separation of isotopes is required is converted into the vapour state.The pressure kept very low 0.000001 to 0.0000001 torr. Then vapour allowed to enter in ionization chamber where fast moving electrons are thron upon them.Then these vapours are ionized.The postively charged ion of isotopes have different masses depending upon the nature of the isotopes presant in them. m/e=H2r2/2E Mass spectrometry (MS) is an analytical method that ionizes chemical species and types the ions based totally on their mass to price ratio. In less difficult phrases, a mass spectrum measures the masses within a pattern. Mass spectrometry is used in many one of a kind fields and is implemented to pure samples as well as complicated combos. A mass spectrum is a plot of the ion signal as a characteristic of the mass-to-fee ratio. these spectra are used to determine the basic or isotopic signature of a pattern, the hundreds of particles and of molecules, and to clarify the chemical structures of molecules, including peptides and different chemical compounds. A mass spectrometer includes three additives: an ion supply, a mass analyzer, and a detector. The ionizer converts a portion of the pattern into ions. there may be a huge variety of ionization strategies, depending on the phase (strong, liquid, fuel) of the pattern and the performance of various ionization mechanisms for the unknown species. An extraction device removes ions from the pattern, which can be then centered through the mass analyzer and onto the detector. The differences in loads of the fragments allows the mass analyzer to kind the ions by their mass-to-price ratio. The detector measures the cost of an indicator quantity and for this reason offers information for calculating the abundances of every ion gift. some detectors also supply spatial data, e.g., a multichannel plate. Time-of-flight For more details on this subject matter, see time-of-flight mass spectrometry. The time-of-flight (TOF) analyzer uses an electric subject to accelerate the ions through the identical ability, after which measures the time they take to reach the detector. If the particles all have the same rate, the kinetic energies might be same, and their velocities will rely most effective on their hundreds.sabaqpk. Lighter ions will attain the detector first Mass spectrometry produces various forms of records. The maximum commonplace records illustration is the mass spectrum. positive kinds of mass spectrometry facts are quality represented as a mass chromatogram.Sabaq.pk. types of chromatograms include selected ion monitoring (SIM), general ion contemporary (TIC), and selected response monitoring (SRM), among many others. other varieties of mass spectrometry data are properly represented as a 3-dimensional contour map. in this form, the mass-to-fee, m/z is on the x-axis, intensity the y-axis, and an extra experimental parameter, inclusive of time, is recorded at the z-axis What is Molecule|Chemistry Notes Class 11| in URDU/HINDI|: https://www.youtube.com/watch?v=WItay3HeLd8 What is Atom and its Structure|Chemistry Notes Class 11| in URDU/HINDI|: https://www.youtube.com/watch?v=IvC8XkS5APA Avidence of Atom |Chemistry Notes Class 11| in URDU/HINDI|: https://www.youtube.com/watch?v=GY6GlQ9WIPs What is an Ion |Chemistry Notes Class 11| in URDU/HINDI|: https://www.youtube.com/watch?v=hTrp1tsgct8 Please Subcribe my Channal: https://www.youtube.com/channel/UCIKPHuv7Exg6JA8rTNfXghQ?sub_confirmation=1 Mass Spectrometry Analysis | Mass Spectrometr | Chemistry Notes Class 11| in URDU/HINDI | Thanks.....
Views: 10889 Gamer Master Academy
Quadrupole Mass Spectrometer Working Principle Animation - How to Measure Vacuum
 
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The quadrupole mass spectrometer (QMS) is used to detect and measure the abundance of gas phase ions. These ions have to pass between electrically connected rods in order to reach the detector. By combining alternating and direct voltage on these rods, it is possible to ensure that only ions with specific mass-to-charge ratio are capable of reaching the detector. Channel: https://www.youtube.com/c/MaidoMerisalu Facebook: https://www.facebook.com/CaptainCorrosion/ Website: http://captaincorrosion.com/
Views: 80463 Captain Corrosion
Quantitative Mass Spectrometry Sample Prep for New and Experienced Users
 
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A description of the rationale, considerations, and general techniques used to prepare samples for proteomic MS analysis, as well as an overview of methods for reducing sample complexity and tools for improving sample preparation reproducibility.
A Brief Introduction to Mass Spectrometry
 
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A brief overview of a simple EI-mode mass spectrometry experiment.
Views: 176925 ChemSurvival
Gas Chromatography/Mass Spectrometry
 
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Gas Chromatography Mass Spectrometry, or GC/MS, is an analytical technique used in a variety of different forensic disciplines; for example, drug chemistry, toxicology, and trace chemistry. Learn all about it right here! Visit NFSTC at http://www.nfstc.org
Views: 56211 NFSTC at FIU
Lecture 4. Mass Spectrometry: Theory, Instrumentation, and Techniques
 
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This video is part of a 28-lecture graduate-level course titled "Organic Spectroscopy" taught at UC Irvine by Professor James S. Nowick. The course covers infrared (IR) spectroscopy, mass spectrometry, and nuclear magnetic resonance (NMR) spectroscopy, the latter of which is the main focus. Topics covered in the NMR spectroscopy part of the course include chemical shifts, spin-spin coupling, dynamic effects in NMR spectroscopy, and 2D NMR spectroscopy (COSY, HMQC, HMBC, TOCSY, NOESY, ROESY). Any questions or concerns regarding this class, please e-mail: jsnowick at uci.edu. Copyright © 2011 The Regents of the University of California All Rights Reserved Filmed by the Teaching, Learning, and Technology Center CC-BY-SA
Views: 170384 UCI Media
Theory of MALDI-TOF Mass Spectrometry
 
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Matrix-Assisted Laser Desorption Ionization (MALDI) Time of Flight (TOF) Mass Spectrometry is a versatile method used to analyze the composition of biomolecules and other organic macromolecules. This video is an introduction to the theory of MALDI-TOF spectrometry, including the ionization and detection process, as well as some advantages of MALDI compared with other ionization methods. http://webs.anokaramsey.edu/MALDIEducation “MALDI-based Research-like Experiences in a 2YC/4YC Collaboration with a Renewable Fuels Industry Partner” NSF ATE #1400885
Views: 81621 ARCC Chem
Mass Spectrometry - Fragmentation
 
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See more videos at: http://talkboard.com.au/ In this video, we look at the idea of fragmentation in mass spectrometry. We examine how fragmentation can occur repeatedly with a given substance, and how it helps us to breakdown the structure of a molecule.
Views: 112074 talkboard.com.au
Determination of Relative Atomic Mass by Mass Spectrometry
 
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A simple description of how mass spectrometry is used to determine isotopic abundance for elements followed by the calculation of relative atomic mass
Views: 11872 MaChemGuy
The Impact of Mass Spectrometry on Biomedical Research
 
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Understand the value of accurate and precise measurement in biomedical research. Drs. Peebles and Milne of Vanderbilt University Medical Center highlight how mass spectrometry provides analytical rigor not achievable with immunoaffinity technologies.
Views: 366 Waters Corporation
Liquid Chromatography-Tandem Mass Spectropmetry (LC-MS/MS)
 
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Edited from original video by Agilent Technologies https://www.youtube.com/watch?v=DRo_VglHWZg
Views: 48062 Said Abd El-Monem
Gas Chromatography | working principle and instrumentation lecture
 
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Gas chromatography lecture - This chromatography lecture explains about the instrumentation, principle of gas chromatography. Gas chromatography (GC) is a common type of chromatography used in analytical chemistry for separating and analyzing compounds that can be vaporized without decomposition. Typical uses of GC include testing the purity of a particular substance, or separating the different components of a mixture (the relative amounts of such components can also be determined). In some situations, GC may help in identifying a compound. In preparative chromatography, GC can be used to prepare pure compounds from a mixture. This lecture will explain the principle of gas chromatography and the instrumentation and uses of gas chromatography. In gas chromatography, the mobile phase (or "moving phase") is a carrier gas, usually an inert gas such as helium or an unreactive gas such as nitrogen. Helium remains the most commonly used carrier gas in about 90% of instruments although hydrogen is preferred for improved separations.The stationary phase is a microscopic layer of liquid or polymer on an inert solid support, inside a piece of glass or metal tubing called a column (an homage to the fractionating column used in distillation). The instrument used to perform gas chromatography is called a gas chromatograph (or "aerograph", "gas separator"). Gas chromatography is in principle similar to column chromatography (as well as other forms of chromatography, such as HPLC, TLC), but has several notable differences. First, the process of separating the compounds in a mixture is carried out between a liquid stationary phase and a gas mobile phase, whereas in column chromatography the stationary phase is a solid and the mobile phase is a liquid. (Hence the full name of the procedure is "Gas–liquid chromatography", referring to the mobile and stationary phases, respectively.) Second, the column through which the gas phase passes is located in an oven where the temperature of the gas can be controlled, whereas column chromatography (typically) has no such temperature control. Finally, the concentration of a compound in the gas phase is solely a function of the vapor pressure of the gas. Gas chromatography is also similar to fractional distillation, since both processes separate the components of a mixture primarily based on boiling point (or vapor pressure) differences. Gas chromatography is also sometimes known as vapor-phase chromatography (VPC), or gas–liquid partition chromatography (GLPC). These alternative names, as well as their respective abbreviations, are frequently used in scientific literature. Strictly speaking, GLPC is the most correct terminology, and is thus preferred by many authors. In most modern GC-MS systems, computer software is used to draw and integrate peaks, and match MS spectra to library spectra. Gas Chromatography is used extensively in forensic science. Article source: wikipedia I don't own this article written in the description. © goes to original content developers from Wikipedia. For more information, log on to- http://www.shomusbiology.com/ Get Shomu's Biology DVD set here- http://www.shomusbiology.com/dvd-store/ Download the study materials here- http://shomusbiology.com/bio-materials.html Remember Shomu’s Biology is created to spread the knowledge of life science and biology by sharing all this free biology lectures video and animation presented by Suman Bhattacharjee in YouTube. All these tutorials are brought to you for free. Please subscribe to our channel so that we can grow together. You can check for any of the following services from Shomu’s Biology- Buy Shomu’s Biology lecture DVD set- www.shomusbiology.com/dvd-store Shomu’s Biology assignment services – www.shomusbiology.com/assignment -help Join Online coaching for CSIR NET exam – www.shomusbiology.com/net-coaching We are social. Find us on different sites here- Our Website – www.shomusbiology.com Facebook page- https://www.facebook.com/ShomusBiology/ Twitter - https://twitter.com/shomusbiology SlideShare- www.slideshare.net/shomusbiology Google plus- https://plus.google.com/113648584982732129198 LinkedIn - https://www.linkedin.com/in/suman-bhattacharjee-2a051661 Youtube- https://www.youtube.com/user/TheFunsuman Thank you for watching gas chromatography lecture
Views: 243078 Shomu's Biology
Chem 3440 Mass Spectrometric Measurements Experiment
 
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03:09 Login Info 07:15 Purging the Catalyst 25:23 Day 2: Mechanism of Adsorption Mass Spectrometric Measurements of Heterogeneous Catalysis
Views: 359 U of I Chemistry
Mass spectrometric methods for the direct elemental and isotopic analysis of solid material
 
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A A Ganeev, A R Gubal, S V Potapov, N N Agafonova, V M Nemets, "Mass spectrometric methods for the direct elemental and isotopic analysis of solid material", RUSS CHEM REV, 2016, 85 (4), 427–444 DOI: http://dx.doi.org/10.1070/RCR4504 Video abstract of the paper
Views: 61 Dmitry Tcheboukov
IB Chemistry Topic 11.3 Spectroscopic identification of organic compounds
 
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IB Chemistry Topic 11.3 Spectroscopic identification of organic compounds How to read graphs from HNMR, mass, and IR spectroscopy and determine IHD. Full set of resources for topic 11/21: http://www.mrwengibchemistry.com/topic-11-measurement.html 0:26 Instrument overview and use of EMS 0:44 EMS formulas 1:14 Infrared IR spectroscopy 5:16 Proton nuclear magnetic resonance H1 NMR spectroscopy 10:11 Index of hydrogen deficiency IHD 13:29 Mass spectrometry MS ​11.3 Spectroscopic identification of organic compounds The degree of unsaturation or index of hydrogen deficiency (IHD) can be used to determine from a molecular formula the number of rings or multiple bonds in a molecule. Mass spectrometry (MS), proton nuclear magnetic resonance spectroscopy (1H NMR) and infrared spectroscopy (IR) are techniques that can be used to help identify compounds and to determine their structure. Determination of the IHD from a molecular formula. Deduction of information about the structural features of a compound from percentage composition data, MS, 1H NMR or IR. Connect with me: Facebook: https://www.facebook.com/IBChemistry2016/ Twitter: https://twitter.com/andrewweng0406 Google plus: https://plus.google.com/u/0/108611113268141564345 Pinterest: https://www.pinterest.com/mrandrewweng040/ib-chemistry/
Views: 6807 Andrew Weng
MALDI Imaging: A live system demonstration
 
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The latest development in Tissue Imaging technologies is "MALDI Imaging", a system that gives access to the mass spectrometric analysis of proteins and peptides of a tissue section. Even small molecules can be analyzed. The MALDI Molecular Imager is a unique integrated discovery platform to provide the researcher with all tools for successful MALDI Imaging experiments.
Views: 22005 MCBDAL
Applications of Mass Spectrometry
 
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Subject:Analytical Chemistry/Instrumentation Paper: Atomic spectroscopy
Views: 259 Vidya-mitra
Ion Mobility/Mass Spectrometry for Metabolomics and Clinical Research Analysis
 
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Ion Mobility/Mass Spectrometry for Metabolomics and Clinical Research Analysis Presented by: LabRoots Speaker: Richard Yost, PhD - Colonel Allen R. and Margaret G. Crow Professor and Head, Analytical Chemistry, University of Florida; Director, NIH Southeast Center for Integrated Metabolomics Speaker Biography: Dr. Yost is the Colonel Allen R. and Margaret G. Crow Professor and Head of Analytical Chemistry at the University of Florida. He is recognized internationally as a leader in the field of analytical chemistry, particularly tandem mass spectrometry (MS/MS). He may be best known for inventing (as a graduate student with Chris Enke at Michigan State University) the triple quadrupole mass spectrometer, which 40 years later represents over $1B in sales each year. Dr. Yost's professional activities have focused on research and teaching in analytical mass spectrometry, particularly tandem mass spectrometry (MS/MS). His group's research has reflected a unique balance between instrumentation development, fundamental studies, and applications in analytical chemistry. His group has led in the application of novel mass spectrometric methods and techniques to areas such as metabolomics, clinical, biomedical, pharmaceutical, environmental, and forensic chemistry. Dr. Yost has supervised the research of well over 100 graduate students during the past 37 years, graduating over 85 PhDs from his group. He has served as PI or Co‐PI on grants and contracts totaling over $50M of funding. Research in the group has led to almost 200 publications and 16 patents. He still loves teaching undergraduates and graduates in the classroom each semester. Dr. Yost recently completed terms on the Florida Board of Governors (Regents) and the University of Florida Board of Trustees. He is director of the NIH‐funded Southeast Center for Integrated Metabolomics. He is also a Professor of Pathology at the University of Florida. His research has been recognized with the highest award in his discipline, the 1993 ASMS Award for Distinguished Contribution in Mass Spectrometry, as well as the 2018 MSACL Award for Distinguished Contribution in Clinical Mass Spectrometry. He currently serves as the VP for Programs of ASMS, and will become President in July. Webinar: Ion Mobility/Mass Spectrometry for Metabolomics and Clinical Research Analysis Abstract: Ion mobility/mass spectrometry has tremendous potential for metabolomics, lipidomics, and clinical analysis. Ion mobility can resolve compounds unresolved by LC/MS/MS, provide additional structural information not available from mass spectrometry, and reduce or eliminate the need for chromatographic separation. These features offer significant improvements for quantitative targeted metabolomics and clinical research analysis, as well as for untargeted (global) metabolomics studies. This presentation will explore innovations in ion mobility/mass spectrometry for metabolomics, lipidomics, and clinical research analysis. Techniques to be covered include both classic drift tube ion mobility (IMS) and high‐field asymmetric‐waveform ion mobility (FAIMS), in conjunction with HRMS, MS/MS, and LC/MS. Characterization and optimization of instrumental parameters critical for analytical performance will be explored, including ionization techniques, cationization and complexation of analytes for improved mobility separation, and integration with chromatographic separation and MS/MS. Applications will include a range of metabolomics, lipidomics, and targeted clinical research analyses. Specific examples will include rapid clinical research assays (vitamin D and its epimers), separation of isomeric performance‐enhancing steroids, breath analysis research for potential early disease screening, and improvements in mass spec imaging. Recent advances in these areas will be highlighted, along with a perspective on the metabolomics and clinical future of these approaches. Learning Objectives: - To understand how ion mobility is combined with mass spectrometry - To understand how in mobility/mass spectrometry can be used for clinical research analysis and metabolomics Sponsored by: Agilent Earn PACE Credits: 1. Make sure you’re a registered member of LabRoots: https://www.labroots.com/webinar/ion-mobility-mass-spectrometry-metabolomics-clinical-analysis 2. Watch the webinar on YouTube or on the LabRoots Website: https://www.labroots.com/webinar/ion-mobility-mass-spectrometry-metabolomics-clinical-analysis 3. Click Here to get your PACE credits 4/30/2020: http://www.labroots.com/credit/pace-credits/2817/third-party LabRoots on Social: Facebook: https://www.facebook.com/LabRootsInc Twitter: https://twitter.com/LabRoots LinkedIn: https://www.linkedin.com/company/labroots Instagram: https://www.instagram.com/labrootsinc Pinterest: https://www.pinterest.com/labroots/ SnapChat: labroots_inc
Views: 128 LabRoots
Mass Spectrometry: Fragmentation Mechanisms
 
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Looks at the major fragmentation mechanisms of the mass spec molecular ion. Works full mechanism of inductive/heterolytic cleaveage, alpha/homolytic cleavage, McClafferty Rearrangements, and loss of water.
Mass Spectrometry Sample Prep for New and Experienced Users - Ryan Bomgarden
 
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While mass spectrometers have improved rapidly over the past few decades, results have remained largely dependent on the quality of the sample, and, by extension, sample preparation that is undertaken for analysis. Part 1 of this webinar will describe the rationale, considerations, and general techniques used to prepare samples for proteomic MS analysis. Additionally, we will also provide an overview of methods for reducing sample complexity and tools for improving proteomics sample preparation reproducibility.
Views: 136 Omics Research
Mass Spectrometry for Biological Research and Network Medicine Applications
 
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Learn from Lorne Taylor about Mass Spectrometry for Biological Research and Network Medicine Applications.
Views: 1572 SCIEX
OpenChrom - Mass Spectrum Selection
 
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OpenChrom is an open source software for mass spectrometric chromatography. The version 0.4.0 "Tswett" is available at: http://www.openchrom.net/main/content/downloads.php
Views: 3430 TheEselmeister
[FIRST freeware Mass++] Overview of Mass++ video tutorial
 
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■Project "Development of the next generation mass spectrometry system, and contribution toward drug discovery and diagnostics" supported by Funding Program for World-Leading Innovative R&D on Science and Technology (FIRST) ■About this video This is the "Overview of Mass++" video tutorial for the free mass spectrometry analysis software Mass++. In this video tutorial, we introduce the following functions' overviews : (1) File Open and Peak Detection.....0:03~ (2) Mascot Search (MS/MS Ion Search)......0:53~ (3) MassBank Search......1:23~ (4) Differential Analysis ......2:19~ Note: ・The detail video tutorials of MassBank Search has released: http://youtu.be/vINNT86VAO0 ・The detail video tutorials of each function will be released later. ■Further details and Mass++ download Japanese: http://www.first-ms3d.jp/achievement/software English: http://www.first-ms3d.jp/english/achievement/software This video tutorial can be downloaded in Flash format (which includes hyperlink buttons such as "Display undisplayed panes") from: Japanese: http://www.first-ms3d.jp/mass2-tutorial English:http://www.first-ms3d.jp/english/mass2-tutorial
Views: 898 firstms3d
Experiment 8.6 Mass Spectrometry to characterize PTM proteins
 
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Characterization of the proteins that were stained with the PTM specific dyes for further analysis
Views: 656 Darpan Malhotra
Simplifying Mass Spectrometry Method Development for Food and Environmental Analysis
 
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In this video, Senior Scientist Dimple Shah explains how Waters Quanpedia database can be used to accelerate and simplify mass spectrometry data management in the analysis of food and environmental contaminants. http://www.waters.com/quanfe
Views: 435 Waters Corporation
Mass Spectrometry for Biopolymer/BioPharmaceutical Characterisation
 
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Fiona Greer (SGS M-Scan, UK) To register to view the full version of this presentation visit http://view6.workcast.net/register?cpak=2274999072143499 Following an introduction to the main mass spectrometric techniques for protein and carbohydrate analysis (On-line LC/MS, MALDI-TOF MS and GC-MS), examples will be shown of their use in the structural characterisation of biopharmaceutical products ranging from synthetic peptides to antibody molecules. Details will be provided as to which combination of MS techniques and preparative chemistry is most appropriate for peptide, protein, carbohydrate and oligonucleotide characterisation. Particular reference will be made to the ability of each technique to deal with heterogeneous mixtures and post-translational modifications such as glycosylation, phosphorylation, sulphation, oxidation and deamidation. An introduction to the concept of collision induced dissociation tandem MS/MS analysis for de-novo protein sequencing will be given. Participants will gain an understanding of the different types of ionisation methods and mass spectrometers best suited to the study of Biopolymer structural characterisation and protein sequencing.
Views: 632 Separation Science
Trypsin digestion
 
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For more information, log on to- http://shomusbiology.weebly.com/ Download the study materials here- http://shomusbiology.weebly.com/bio-materials.html Trypsin digestion or in-gel digestion is part of the sample preparation for the mass spectrometric identification of proteins in course of proteomic analysis. The method was introduced 1992 by Rosenfeld.[1] Despite innumerable modifications and improvements the basic elements of the procedure remain largely unchanged. The in-gel digestion primarily comprises the four steps destaining, reduction and alkylation (R&A) of the cysteines in the protein, proteolytic cleavage of the protein and extraction of the generated peptides. Afterwards the eponymous step of the method is performed, the in-gel digestion of the proteins. By this procedure, the protein is cut enzymatically into a limited number of shorter fragments. These fragments are called peptides and allow for the identification of the protein with their characteristic mass and pattern. The serine protease trypsin is the most common enzyme used in protein analytics. Trypsin cuts the peptide bond specifically at the carboxyl end of the basic aminoacids arginine and lysine. If there is an acidic amino acid like aspartic acid or glutamic acid in direct neighborhood to the cutting site, the rate of hydrolysis is diminished, a proline C-terminal to the cutting site inhibits the hydrolysis completely.[21] An undesirable side effect of the use of proteolytic enzymes is the self digestion of the protease. To avoid this, in the past Ca2+-ions were added to the digestion buffer.[22][23] Nowadays most suppliers offer modified trypsin where selective methylation of the lysines limits the autolytic activity to the arginine cutting sites.[24] Unmodified trypsin has its highest activity between 35°C and 45°C. After the modification, the optimal temperature is changed to the range of 50°C to 55°C.[15][25] Other enzymes used for in-gel digestion are the endoproteases Lys-C,[26][27][28] Glu-C,[29][30][31] Asp-N [32] and Lys-N.[33][34] These proteases cut specifically at only one amino acid e.g. Asp-N cuts n-terminal of aspartic acid.[26] Therefore a lower number of longer peptides is obtained. The analysis of the complete primary sequence of a protein using only one protease is usually not possible. In those cases the digestion of the target protein in several approaches with different enzymes is recommended. The resulting overlapping peptides permit the assembly of the complete sequence of the protein.[29][35][36] For the digestion the proteins fixed in the matrix of the gel have to be made accessible for the protease. The permeation of the enzyme to the gel is believed to be facilitated by the dehydration of the gel pieces by treatment with acetonitrile and subsequent swelling in the digestion buffer containing the protease. This procedure relies on the presumption that the protease permeates to the gel by the process of swelling.[37] Different studies about the penetration of the enzymes to the gel showed the process to be almost completely driven by diffusion. The drying of the gel does not seem to support the process.[6][15] Therefore, the improvement of the in-gel digestion has to be achieved by the reduction of the way of the enzyme to its substrate e.g. by cutting the gel to pieces as small as possible. Usually, the in-gel digestion is run as an overnight process. For the use of trypsin as protease and a temperature of 37°C the time of incubation found in most protocols is 12-15 h. However, experiments about the duration of the digestion process showed that after 3 h there is enough material for successful mass spectrometric analysis.[38] Furthermore, the optimisation of the conditions for the protease in temperature and pH allows for the completion of the digestion of a sample in 30 min.[15] Surfactant (detergents) can aid in the solubilization and denaturing of proteins in the gel and thereby shorten digestion times and increase protein cleavage and the number and amount of extracted peptides, especially for lipophilic proteins such as membrane proteins. Cleavable detergents are detergents that are cleaved after digestion, often under acidic conditions. This makes the addition of detergents compatible with mass spectrometry.
Views: 25906 Shomu's Biology
Introduction to Mass Spectrometry
 
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PDF: http://www.mediafire.com/?b49d624iub6k22i
Views: 103705 Alex Baklajian
Our mass spectrometry lab at the University of Cincinnati
 
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A quick trip through our Mass Spec lab
Views: 886 robert ross
Top Ten Medical Innovations: #3 - Mass Spectrometry for Bacterial Identification
 
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Learn about Mass Spectrometry for Bacterial Identification, the 3rd top medical innovation from the Cleveland Clinic. The rapid identification of microorganisms has been a major obstacle to clinicians as they struggle to provide appropriate antimicrobial treatment while waiting sometimes days for a definitive identification of the pathogen. Now, a new method has emerged that can reduce identification to a few minutes. Mass Spectrometry (MS) is a technique used to screen simultaneously a multitude of molecules and determine their identity by analyzing their individual mass-to-charge ratio. These molecular "signatures" can be used for rapid bacterial and fungal identification (ID) from isolated colonies.
Views: 8185 Cleveland Clinic
Pittcon 2012 - Imaging Mass Spectrometry - Abstract 1
 
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TITLE: Molecular Signaling Studied with High Resolution Imaging MS SPEAKER: Ron MA Heeren - FOM-AMOLF ABSTRACT OVERVIEW: Key questions in analytical biology and biochemistry evolve around the determination of three basic molecular properties: molecular composition, molecular structure and molecular localization. The complex interplay between molecules in living systems results in a continuous alteration of these properties at the molecular level. Multimodal biomolecular imaging mass spectrometry combined with quantitative proteomics offers the possibility to perform an in-depth study of biomolecular distributions on complex surfaces. Biomedical applications are currently a major driving force for the rapid development of this field of science. A direct insight in endogenous metabolic pathways as well as pharmacokinetic mechanisms generates a significant amount of interest in the technology. New high performance mass spectrometric technologies such as ion mobility mass spectrometry and high field FTICR-MS are providing more detail on structural identities of molecules observed in pathological tissue sections. We will show how these new developments in imaging MS can elucidate molecular signalling pathways in diseases, single cells and bacterial cultures.
Views: 2470 Pittcon Videos
mMass - Personal Sequence Database
 
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Sequence database tutorial for mMass software. mMass presents an open source cross-platform environment for precise analysis of mass spectrometric data. Available for free at http://www.mmass.org
Views: 1536 martinstrohalm
mMass Screencast - Protein Identifications
 
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Protein identification tutorial for mMass software. mMass presents an open source cross-platform environment for precise analysis of mass spectrometric data. Available for free at http://www.mmass.org
Views: 5889 martinstrohalm
How to draw a Mass Spectrum Graph - IB
 
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Here's a little help for my International Baccaularate and my University buddies - just some basic help for Mass Spectometry. Hope it helps.
Views: 7956 indianaintasian
Sample Prep Liquid Chromatography Made Easy
 
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http://www.thermoscientific.com/prelude -- Jenny Olsen introduces the Thermo Scientific* Prelude SPLC System that makes LC/MS accessible to clinical research and forensic toxicology labs with high efficiency multiplexing, TurboFlow* on-line sample clean up, and chromatographic separation. Practical, economically viable LC/MS analysis is now available with the Thermo Scientific Prelude SPLC Sample Preparation and Liquid Chromatography system. Combined with a Thermo Scientific MS system, the Prelude SPLC system enables fast, reproducible and reliable on-line clean up, high performance chromatographic separation and mass spectrometric analysis of complex biological samples. -- http://www.thermoscientific.com/prelude
Views: 913 Thermo Scientific
mMass Screencast - ESI MS of Proteins
 
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Tutorial on protein ESI MS data processing in mMass software. mMass presents an open source cross-platform tool for precise analysis of mass spectrometric data. Available for free at http://www.mmass.org
Views: 4537 martinstrohalm