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Finding the molecular formula from a mass spectrum
 
17:33
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: 134425 Gary Mabbott
Mass Spectrometry MS
 
07:59
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
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: 261909 Andrew Crookell
Mass spectrometry part 1 : introduction
 
24:09
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: 215202 Shomu's Biology
Simple explanation of the Mass Spectrometer.
 
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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: 329945 FranklyChemistry
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: 176 LabRoots
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: 11382 Gamer Master Academy
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: 243633 Bozeman Science
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: 3524 TheEselmeister
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: 370 U of I Chemistry
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: 53275 Said Abd El-Monem
Mass Spectrometry Sample Prep for New and Experienced Users - Ryan Bomgarden
 
01:07:01
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: 142 Omics Research
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: 83816 Captain Corrosion
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: 3169 FHCRCSharedResources
Quantitative Mass Spectrometry Sample Prep for New and Experienced Users
 
01:07:01
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.
From Discovery to Validation, Trends in Biological Mass Spectrometry
 
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Manfred Raida (Proteomics.Asia, Singapore) To register to view the full version of this presentation visit http://view6.workcast.net/register?cpak=2274999072143499 Targeted approaches are based on the knowledge about the biological systems to be studied. Selection of candidates to be monitored is carried out by orthogonal experiments, as determination of expression level by mRNA analysis, or they are taken from literature. To identify and quantify the finally present proteins proteotypic tryptic peptides are selected and monitored in the complex mixture of all or a subset of the proteins after tryptic digestion. The method for this specific monitoring was taken from the analysis of small molecules or drugs in complex biological fluids, the multiple- or single-reaction-monitoring (SRM or MRM). This presentation will discuss the selection of proteotypic peptides by independent experiments or software tools, the setup of the analysis method and the analysis of the data. To register to view the full version of this presentation visit http://view6.workcast.net/register?cpak=2274999072143499
Views: 369 Separation Science
Mass spectrometry part 5: Graph analysis
 
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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 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: 39169 Shomu's Biology
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: 116797 talkboard.com.au
Spectrometry | Chemistry for All | The Fuse School
 
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Learn the basics about Spectrometry. What is spectometry and its use? Find out more in this video! This Open Educational Resource is free of charge, under a Creative Commons License: Attribution-NonCommercial CC BY-NC ( View License Deed: http://creativecommons.org/licenses/by-nc/4.0/ ). You are allowed to download the video for nonprofit, educational use. If you would like to modify the video, please contact us: [email protected] SUBSCRIBE to the Fuse School YouTube channel for many more educational videos. Our teachers and animators come together to make fun & easy-to-understand videos in Chemistry, Biology, Physics, Maths & ICT. This video is part of 'Chemistry for All' - a Chemistry Education project by our Charity Fuse Foundation - the organisation behind The Fuse School. These videos can be used in a flipped classroom model or as a revision aid. Find our other Chemistry videos here: https://www.youtube.com/playlist?list=PLW0gavSzhMlReKGMVfUt6YuNQsO0bqSMV Twitter: https://twitter.com/fuseSchool Access a deeper Learning Experience in the Fuse School platform and app: www.fuseschool.org Follow us: http://www.youtube.com/fuseschool Friend us: http://www.facebook.com/fuseschool
A Brief Introduction to Mass Spectrometry
 
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A brief overview of a simple EI-mode mass spectrometry experiment.
Views: 182325 ChemSurvival
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: 88339 ARCC Chem
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: 22170 MCBDAL
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: 6088 martinstrohalm
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: 69 Dmitry Tcheboukov
A.2 Inductively coupled plasma mass spectrometry (SL)
 
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Understandings: Trace amounts of metals can be identified and quantified by ionizing them with argon gas plasma in Inductively Coupled Plasma (ICP) Spectroscopy using Mass Spectroscopy ICP-MS and Optical Emission Spectroscopy ICP-OES​. Applications and skills: Explanation of the plasma state and its production in ICP- MS/OES. Identify metals and abundances from simple data and calibration curves provided from ICP-MS and ICP-OES. Explanation of the separation and quantification of metallic ions by MS and OES. Uses of ICP-MS and ICP-OES. Guidance: Details of operating parts of ICP-MS and ICP-OES instruments will not be assessed. Only analysis of metals should be covered. The importance of calibration should be covered.
Views: 12955 Mike Sugiyama Jones
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: 60186 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: 173075 UCI Media
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: 27054 Shomu's Biology
Experiment 6.6 Zip-Tipping and MALDI-TOF/TOF Analysis
 
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Mass Spectrometric analysis of the protein spots showing a positive reaction towards the auto-antibodies. The proteins are extracted from human tumor tissues and the antibodies are from the human serum.
Views: 2009 Darpan Malhotra
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: 641 Separation Science
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: 378 Waters Corporation
Mass spectrometry Animation
 
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Mass spectrometry Animation
Views: 158898 scindiaprem
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: 1581 SCIEX
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: 491 Waters Corporation
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.
Our mass spectrometry lab at the University of Cincinnati
 
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A quick trip through our Mass Spec lab
Views: 908 robert ross
Purushottam Chakraborty | India | Mass Spectrometry 2015 | Conference Series LLC
 
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International Summit on Current Trends in Mass Spectrometry July 13-15, 2015 New Orleans, USA Title: High-resolution MCsn+ - SIMS: an innovative mass spectrometric technique for compositional analysis of quantum structures without ‘standards’ Click here for Abstract and Biography: http://www.massspectra.com/speaker/2015/purushottam-chakraborty-saha-institute-of-nuclear-physics-india OMICS International: http://conferenceseries.com/ OMICS open access Journals: http://omicsonline.org Global Medical Conferences: http://conferenceseries.com Global Pharmaceutical Conferences: http://pharmaceuticalconferences.com Global Cancer Conferences: http://cancersummit.org Global Diabetes Conferences: http://diabetesexpo.com Global Dental Conferences: http://dentalcongress.com Global Nursing Conferences: http://nursingconference.com
Quantitation and profiling metabolomics and translation to clinical analysis
 
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Presented By: Timothy J Garrett, PhD - Associate Professor, University of Florida Speaker Biography: Dr. Garrett received his undergraduate degree from the University of Georgia in Chemistry graduating Summa Cum Laude with Highest Honors (1999). As an undergraduate, he worked in the lab of Dr. I. Jonathan Amster on the characterization of bacterial proteins using MALDI-TOF completing an undergraduate honors thesis entitle "Improved methods for on-probe cleanup of unpurified protein samples for MALDI time-of-flight mass spectrometry". He received his PhD in 2006 from the University of Florida working under the direction of Dr. Richard A. Yost. As a graduate student, he developed the first imaging mass spectrometry based on ion trap instrumentation through a partnership with Thermo and studied the disposition of phospholipids in brain tissue. Webinar: Quantitation and profiling metabolomics and translation to clinical analysis Speaker Biography: Measurement of these metabolites represents the digital readout of health. A key aspect of metabolomics is the utilization of high resolution mass spectrometric approaches to detect and identify metabolites from biological fluids and tissues. The use of multi-analyte analyses as well as high resolution mass spectrometric approaches has the potential to transform clinical diagnostics for the next generation. This presentation will discuss profiling and quantitative metabolomics techniques such as traditional LC-MS based approaches and new methods that utilize direction analysis approaches. Learning Objectives: -Demonstrate the use of multianalyte metabolomic panels in clinical research -Discuss the application of high resolution mass spectrometry approaches to metabolomics -Understand the utilization of bioinformatic tools for interpreting results. Sponsored By: Agilent Earn PACE Credits: 1. Make sure you’re a registered member of LabRoots (https://www.labroots.com/ms/webinar/quantitation-profiling-metabolomics-translation-clinical-analysis) 2. Watch the webinar on YouTube or on the LabRoots Website (https://www.labroots.com/ms/webinar/quantitation-profiling-metabolomics-translation-clinical-analysis) 3. Click Here to get your PACE credits (Expiration date – June 29, 2020 08:00 AM) - https://www.labroots.com/credit/pace-credits/2911/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: 35 LabRoots
Hupo lunch seminar with Prof. Matthias Mann
 
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“Perspectives of clinical proteomics for precision medicine and the resulting demands on front-end separation for mass spectrometric analysis.”, Professor Matthias Mann, MPI, Martinsried
Views: 96 Evosep
mMass Screencast - Spectrum Viewer
 
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Basic spectrum manipulations 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: 6931 martinstrohalm
Advion Launches LESA (Liquid Extraction Surface Analysis) via TriVersa NanoMate
 
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Advion BioSystems Announces the Launch of a Novel Liquid Extraction Surface Analysis System ITHACA, NY, USA, March 1, 2010 — Advion BioSystems, Inc. (Advion) announces the launch of its Liquid Extraction Surface Analysis (LESA) sample analysis system. LESA, based on Advions chip-based nanoelectrospray platform, the TriVersa NanoMate®, will be used to provide direct Mass Spectrometric analysis of a variety of sample formats including tissue and organ samples, Thin Layer Chromatography (TLC) plates, MALDI plates, and Dried Blood Spots (DBS). The direct analysis of surfaces by mass spectrometry is a growing and powerful technique. The novel approach and design of the Advion LESA system enables, for the first time, the ability to couple direct analysis of surfaces with the power and breadth of chip-based nanoelectrospray. This simple-to-use combination allows for soft ionization, thereby preserving fragile molecules such as phase 2 metabolites and allowing unrivalled detection of drugs and their metabolites in tissue and organ samples. Researchers developing new forensic tools, novel drugs, better biofuels and technologies to strengthen homeland security now have a powerful new tool to use to analyze a variety of surfaces. The new system was developed by Oak Ridge National Laboratory (ORNL), a multiprogram science and technology laboratory managed for the U.S. Department of Energy by UT-Battelle, which exclusively licensed the technology to AB SCIEX, a global leader in life science analytical technologies. In parallel, Advion signed an exclusive sublicense agreement with DH Technologies Development Pte. Ltd., an AB SCIEX affiliate, to commercialize certain discoveries and pending patents that leverage the Advion TriVersa NanoMate product lines used in the ORNL research in conjunction with AB SCIEX mass spectrometers. The launch of this innovative sample analysis system is extremely strategic for our company, said David B. Patteson, CEO of Advion. This is the result of our working closely with ORNL and AB SCIEX dating back nearly seven years to early discussions between Jack Henion our Chairman and CSO and our partners. We expect significant impact from our customers applying this technique to a myriad of sample types and conditions, which to date have been difficult to assay. About Advion BioSystems, Inc. Advion is the scientific leader in microfluidic systems. The companys scientific knowledge base creates unique nanotechnologies delivering speed, flexibility, and exceptional data quality. Advion is the microfluidics supplier of choice for customers demanding scientific excellence, more information from complex samples, and greater throughput. More about the company can be found at www.advion.com. For Advion BioSystems, Inc. Heather Scollins Sr. Marketing Communication Specialist Telephone: +1-607-266-0665, ext. 333 [email protected]
Views: 2410 AdvionBioSciences
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: 7553 Andrew Weng
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: 8316 Cleveland Clinic
mMass Screencast - Lipids Identification
 
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Lipids 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: 2610 martinstrohalm
Mass Spectrometry to find therapeutic drug for liver disease and COPD
 
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Alpha-1 antitrypsin is a protein that is produced in the liver and its role is to protect lung tissue. In people with Alpha 1-antitrypsin deficiency, antitrypsin proteins associate with each other forming polymers, which are damaging to cells. People with this deficiency are likely to suffer from both liver disease and emphysema. Dhawal is using native mass spectrometry to understand how small peptides bind to Alpha-1 antitrypsin and how such peptides prevent polymer formation. Understanding this mechanism will hopefully lead to improved treatments for such a disease.
Views: 150 Suzanne Ruddy
Different parts of the mass spectrometer lab part 1
 
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Bryan showing me different parts of the mass spectrometer lab
Views: 453 NaRuToUzUmAkIthe1st

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