Home
Search results “Mass spectrometric analysis of”
Mass Spectrometry
 
04:51
Who wants to smash molecules into little bits? A mass spectrometer does, that's who. This is a good technique for corroborating molecular structure, because we can make sure the puzzle pieces fit the right way. Check it out! To support this channel and keep up on STEM news at the same time, click on the link below and subscribe to this FREE newsletter: http://www.jdoqocy.com/click-9021241-13591026 Subscribe: http://bit.ly/ProfDaveSubscribe [email protected] http://patreon.com/ProfessorDaveExplains http://professordaveexplains.com http://facebook.com/ProfessorDaveExpl... http://twitter.com/DaveExplains General Chemistry Tutorials: http://bit.ly/ProfDaveGenChem Organic Chemistry Tutorials: http://bit.ly/ProfDaveOrgChem Biochemistry Tutorials: http://bit.ly/ProfDaveBiochem Classical Physics Tutorials: http://bit.ly/ProfDavePhysics1 Modern Physics Tutorials: http://bit.ly/ProfDavePhysics2 Mathematics Tutorials: http://bit.ly/ProfDaveMaths Biology Tutorials: http://bit.ly/ProfDaveBio American History Tutorials: http://bit.ly/ProfDaveAmericanHistory
Views: 161987 Professor Dave Explains
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
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: 255617 Shomu's Biology
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: 171612 Gary Mabbott
Mass Spectrometry Animation | Instrumentation and Working
 
04:15
Link of Complete Lecture: https://www.youtube.com/watch?v=Wc8-GJY42lE Mass Spectrometry, Mass Spectrometry Animation, Instrumentation and Working of Mass Spectrometer, Mass Spectrometer, Instrumentation of Mass Spectrometry, Instrumentation and Working of Mass Spectrometry, Working of Mass Spectrometry, Mass Spectrometry, Ionization Chamber in Mass Spectrometry, Ion Acceleration Chamber, Sampling in Mass Spectrometry, Ionization Potential in Mass Spectrometry, Magnetic Field Deflection Mass Analyser, Time of Flight Mass Analyser, Double Focussing Mass Analyser, Quadrupole Mass Analyser, FT-ICR Mass Analyser.
Views: 30834 Dr. Puspendra Classes
Mass Spectrometry
 
08:20
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: 279205 Bozeman Science
Gas Chromatography/Mass Spectrometry
 
03:09
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: 75218 NFSTC at FIU
Mass spectrometry part 5: Graph analysis
 
17:40
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: 45784 Shomu's Biology
Mass spectrometry part 3 : protein analysis (step by step process)
 
35:56
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: 73987 Shomu's Biology
OpenChrom - Mass Spectrum Selection
 
03:41
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: 4015 TheEselmeister
GCMS  Gas Chromatography Mass Spectrometry
 
22:51
GCMS Gas Chromatography Mass Spectrometry - GoPro Dual Camera view - FPS - IPOV If you would like to have more chemistry fun, and learn about cool science, subscribe to this channel to view the upcoming videos. Thanks for watching and never give up in whatever you do ! REMEMBER: “The beginning is always the hardest” FUN MAN Homepage: https://www.chemistry.nus.edu.sg/people/Teaching_staff/fungfm.htm National University of Singapore: http://www.nus.edu.sg/ Department of Chemistry: https://www.chemistry.nus.edu.sg/index.php “Ever tried. Ever failed. No Matter. Try again. Fail again. Fail better.” - Samuel Beckett LIGHT-HEARTED CHEMISTRY LECTURE SERIES – FUN MAN FLIPPED CLASSROOM Carboxylic Acid Derivative https://www.youtube.com/watch?v=pNa-2B0UwyE Alkene https://www.youtube.com/watch?v=_C2fw0obLdA Inductive – Resonance Effect https://www.youtube.com/watch?v=DajkT2SNwZc VIDEOS ON CHEMISTRY TECHNIQUES IN THE LAB UV Spectroscopy https://www.youtube.com/watch?v=s5uIVQGFDE4 Thin Layer Chromatography https://www.youtube.com/watch?v=iV1GfI_BbKE Flash Column Chromatography https://www.youtube.com/watch?v=ci2uu9Cuf5s NMR Nuclear Magnetic Resonance https://www.youtube.com/watch?v=Tv38vCHcksU Liquid-liquid extraction https://www.youtube.com/watch?v=kdsZjeywrTk Folding Fluted Filter paper https://www.youtube.com/watch?v=hY3XuXa0YuE ChemDraw Pro 15.0 Tutorial https://www.youtube.com/watch?v=037WCSsoivo Schlenk Line https://www.youtube.com/watch?v=Eov60kI7yw8 Glove Box https://www.youtube.com/watch?v=IpTc-qcNPgY
Views: 31576 Fun Man Fung
Sample Preparation for MALDI-TOF Mass Spectrometry
 
09:04
The success of your MALDI-TOF mass spectrometry analysis depends largely on how the sample is prepared. There are a number of choices to be made when preparing a MALDI-TOF sample, each of which has its own advantages and disadvantages. Resources for MALDI-TOF sample preparation: Sigma-Aldrich Analytix Guide to MALDI-Mass Spectrometry: http://www.niu.edu/analyticallab/_pdf/maldi/fl-analytix6-2001.pdf Bruker Guide to MALDI Sample Preparation: https://www.bruker.com/fileadmin/user_upload/8-PDF-Docs/Separations_MassSpectrometry/InstructionForUse/8702557_IFU_Bruker_Guide_MALDI_Sample_Preparation_Revision_E.pdf Sigma-Aldrich List of Matrix Substances for MALDI-MS: http://www.sigmaaldrich.com/analytical-chromatography/analytical-products.html?TablePage=103431784 MALDI-TOF ChemWiki: http://chemwiki.ucdavis.edu/Core/Analytical_Chemistry/Instrumental_Analysis/Mass_Spectrometry/MALDI-TOF UC Irvine MALDI Sample Preparation Guide: http://www.chem.uci.edu/~jgreaves/mass-spectrometry/index.php/sampleprep/93-oamaldi WU St. Louis MALDI Sample Preparation General Recommendations: http://msr.dom.wustl.edu/maldi-sample-preparation-general-recommendations/ MIT MALDI-TOF Sample Preparation Guide: http://web.mit.edu/speclab/www/PDF/DCIF-MALDI_sample_prep.pdf SD State MALDI Sample Preparation Guide: https://www.sdstate.edu/chem/mass-spec/tutorials/upload/Maldi-Sample-Preparation.pdf
Views: 32813 ARCC Chem
Simple explanation of the Mass Spectrometer.
 
04:52
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: 358269 FranklyChemistry
Mass Spectrometry - Fragmentation
 
14:55
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: 130099 talkboard.com.au
Protein Phosphorylation Analysis by Mass Spectrometry
 
05:23
Protein phosphorylation, a reversible process, is characterized by adding phosphate donated from ATP and removing phosphate from a phosphorylated protein substrate. For more information, please visit: https://www.creative-proteomics.com/services/phosphorylation.htm
Views: 550 Creative Proteomics
A Level Chemistry Isotopes and the mass spectrometer
 
06:05
A Level Chemistry Isotopes and the mass spectrometer You can watch all my videos, fully indexed at www.freesciencelessons.co.uk In this video, we explore isotopes, looking at the definition and the idea of relative abundance. We then look at how the time-of-flight mass spectrometer works and how to interpret a mass spectrum. You can expect to see this on your exam. You need to download a copy of the Periodic Table for your exam board from the links below: http://filestore.aqa.org.uk/resources/chemistry/AQA-7404-SDB.PDF http://www.ocr.org.uk/Images/75088-datasheet-specimen.pdf http://qualifications.pearson.com/content/dam/pdf/A%20Level/Chemistry/2015/Specification%20and%20sample%20assessments/AS_Chemistry_2015_Specification.pdf
Views: 61972 Freesciencelessons
Mass spectrometric methods for food fraud analysis
 
02:12
The scientific challenges in moving from targeted to non-targeted mass spectrometric methods for food fraud analysis: A proposed validation workflow to bring about a harmonized approach. Daniele Cavanna & Michele Suman - Barilla Advanced Laboratory Research Laura Righetti - Department of Food and Drug, University of Parma Chris Elliott - Faculty of Medicine, Health & Life Sciences, Queen's University Belfast LINK TO FULL PAPER: https://doi.org/10.1016/j.tifs.2018.08.007 More information on FOODINTEGRITY: https://secure.fera.defra.gov.uk/foodintegrity/index.cfm
Views: 72 Food Integrity
Improving Human Health One Atom at a Time - Biomedical Accelerator Mass Spectrometry
 
43:09
(Visit: http://www.uctv.tv/) Accelerator mass spectrometry (AMS) is a sensitive mass spectrometric method for detecting and quantifying rare long-lived isotopes with high precision. This technique is widely employed in the earth and environmental sciences and is now being applied in the biomedical fields. AMS is primarily used to in the areas of pharmacology and toxicology to investigate the absorption, distribution, metabolism, and excretion of radiolabeled drugs, chemicals, and nutrients, as well as in the detection of chemically modified DNA and proteins in animal models and humans. The exquisite sensitivity (10-18 mol) of AMS allows for the use of low chemical and radioisotope doses and relatively small sample sizes, which enables studies to be performed safely in humans, using exposures that are environmentally or therapeutically relevant. Series: "Field Trip at the Lab: Science on Saturday" [6/2018] [Show ID: 33431]
Reading raw mass spectrometry data in R
 
07:47
This tutorial shows how to access raw mass spectrometry data in R.
Views: 2832 RforProteomics
Simplifying Mass Spectrometry Method Development for Food and Environmental Analysis
 
03:05
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: 685 Waters Corporation
Mass Spectrometry - Fragmentation
 
12:59
What do you get when you blow molecules up? Watch this video to find out. Also find out how fragmentation of molecules can be used to identify a substance and why you have to be POSITIVE about RADICALS.
Views: 32812 Allery Chemistry
Ambient Ionization Mass Spectrometry
 
11:19
Mass spectrometry has long served as an invaluable tool for detection of type and concentration of chemicals present in carefully-prepared laboratory samples. Mass spectrometry analysis sorts, separates and measures sample ions in relation to instrument magnetic and electronic fields. Recent innovations in the technology have vastly increased the utility of mass spectrometry by allowing for measurement under standard environmental conditions ("ambient"), making the instruments far more portable and requiring little or no sample preparation. Applications of this newer technology range from biomedical, food safety, criminal analysis, and national security, to pollution, and far beyond. This wide array of applications is reflected in an equally wide array of acronyms for the types of ambient ion mass spectrometry. The alphabet soup includes DART ("direct analysis in real time"), DESI ("desorption electrospray ionization"), ASAP ("ambient samples analysis probe"), APPI ("atmospheric-pressure photoionization"), EASI ("easy ambient sonic-spray ionization"), LAESI ("laser ablation electrospray ionization"), ELDI ("electrospray laser desorption ionization"), and "paper spray", to name just a few of the many. This book is the first to bring together in a single work a collection of chapter-length articles by leaders and practitioners in the field ranging widely through the many types, and serves as an excellent gateway to understanding the benefits and uses of this new technology.
Rapid Evaporative Ionization Mass Spectrometry for Direct Food Analysis
 
48:12
In this webinar, learn about the Rapid Evaporative Ionization Mass Spectrometry (REIMS) technique and its applicability to food profiling and authenticity testing. Hosted by Spectroscopy Solutions.
Views: 1159 Waters Corporation
A.2 Inductively coupled plasma mass spectrometry (SL)
 
01:53
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: 22110 Mike Sugiyama Jones
Organic Chemistry II - Solving a Structure Based on IR and NMR Spectra
 
10:27
In this video I determine a plausible chemical structure for an organic compound based on the given IR and H NMR spectra. For a copy of the tables I used, click here: https://drive.google.com/open?id=0BwOceMKQTVFxRTh1Szl4aTh0eE0
Views: 198939 Tony St. John
Ion Mobility/Mass Spectrometry for Metabolomics and Clinical Research Analysis
 
46:24
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: 423 LabRoots
Bottom-up  proteomics and top-down proteomics
 
05:23
Proteomics studies play an increasing role in the field of biology. The use of mass spectrometry (MS) in combination with a range of separation methods is the main principal methodology for proteomics. The two principal approaches to identifying and characterizing proteins using MS are the “bottom-up”, which analyze peptides by proteolytic digestion, and “top-down”, which analyze intact proteins.
Views: 3847 Creative Proteomics
Mass spectrometric methods for the direct elemental and isotopic analysis of solid material
 
03:12
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: 83 Dmitry Tcheboukov
Mass Spectrometry for Biopolymer/BioPharmaceutical Characterisation
 
06:06
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: 664 Separation Science
Webinar: Informatics Support For Mass Spectrometry Based Lipidomics Methods
 
35:37
PREMIER Biosoft hosted a complimentary webinar—Informatics Support for MS Based Lipidomics Methods on Oct 24th, 2018. If you missed our webinar check out the recording.
Views: 200 PREMIER Biosoft
Identifying Proteins using Mass Spectrometry
 
04:07
At MRC-LMB, Mark Skehel focuses on the fundamental understanding of biological processes at a molecular level. This enables scientists to gain an insight into diagnosis of disease and potentially treatments.
Views: 6498 Waters Corporation
The Future of Mass Spectrometry in Food Science
 
03:57
Professor Christopher Elliott describes how developments in mass spectrometry enable reliable detection of food fraud, as a result of advances in targeted and untargeted methodologies.
Views: 44 SelectScience
Solving an Unknown Organic Structure using NMR, IR, and MS
 
27:18
In this lesson we learn the steps of solving for an unknown compound when presented with several spectra including mass spectroscopy, IR, proton NMR, and carbon 13 NMR. Support the Channel! Buy The Complete Solving Unknown Spectroscopy Guide Here: https://www.chemcomplete.com/buy-guides Visit us Online: https://www.chemcomplete.com/ Private 1 on 1 Coaching Available, Custom Video Lessons! Learn with us online! https://www.udemy.com/user/matthew-tomney Follow us on social media: https://twitter.com/ChemComplete https://www.facebook.com/chemcomplete
Views: 24094 ChemComplete
Pittcon 2012 - Imaging Mass Spectrometry - Abstract 2
 
29:51
This session was webcast at Pittcon 2012 in Orlando, Florida on Monday, March 12, 2012. TITLE: Aspects of Imaging Mass Spectrometry in Pharmaceutical Applications SPEAKER: Dieter Drexler - Bristol-Myers Squibb ABSTRACT OVERVIEW: Imaging Mass Spectrometry (IMS) is a tool to visualize the relative distribution of endogenous and exogenous molecules directly from thin tissue sections enabling spatial resolution of molecular events. IMS offers the advantage of label-free analysis and distinction of drug and metabolites in tissue samples and provides complementary data to histopathology and imaging techniques based on radio-labeled analytes. Discussed here will be various IMS platforms and their aspects in pharmaceutical applications.
Views: 1007 Pittcon Videos
Sample Prep for Mass Spectrometry
 
45:40
Proper sample preparation for mass spectrometry-based analysis is essential to obtain reproducible and high-quality results. Many factors must be considered when developing sample preparation protocols including source, physical properties complexity, and abundance, among others. To address this complex issue, the editors of Lab Manager have assembled a team of industry experts to discuss some of the latest trends in sample preparation for mass spectrometry.
Views: 708 LabManagerVideos
Flash or Prep Analysis on expression Compact Mass Spectrometer
 
00:06
The expression compact mass spectrometer from Advion is a versatile single quadrupole at the heart of the chemists laboratory. With little modification, the expression CMS can couple to a range of introduction techniques (direct injection, LC/MS, Flash/Prep/SFC, thin-layer chromatography). This animation demonstrates how the CMS acts as the detector for a Flash or PrepLC chromatography system.
Views: 79 AdvionBioSciences
Lecture 4. Mass Spectrometry: Theory, Instrumentation, and Techniques
 
55:22
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: 181278 UCI Media
The Versatility of Mass Spectrometry (MS) for Drug Discovery
 
01:05:38
The development of user-friendly, affordable and versatile mass spec techniques has enabled an increasing acceptance of MS for various applications. Throughout the drug discovery process, mass spec is being used to characterize both small molecules and larger biological entities. Advancements in mass spec technology have led to an increase in sensitivity and new technologies up front of the MS have generated faster and more efficient workflows to maximize the power of a single MS resource. Presenters: Dr. Yuqin Dai - Agilent Technologies Dr. Jennifer Rossi - Agilent Technologies
Views: 494 LabManagerVideos
Pittcon 2012 - Imaging Mass Spectrometry - Abstract 1
 
34:21
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: 2711 Pittcon Videos
Mass Spectrometry Identifies Food Adulteration
 
03:48
Global Food Conference 2014
Views: 231 QUB MOOC
Introduction to Ionization and Fragmentation in Mass Spectrometry
 
08:41
Professor Davis uses pentane to demonstrate the electron impact ionization process and fragmentation patterns in mass spectrometry of alkanes
Views: 89038 ChemSurvival
mMass Screencast - Spectrum Viewer
 
03:37
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: 7488 martinstrohalm
New Applications on Triple Quadrupole and Q-TOF Instruments with iFunnel Technology
 
01:11:44
Significant gains in LC/MS performance require a fundamental rethinking of atmospheric ion creation and sampling. This webinar introduces iFunnel Technology, which creates and samples many more ions to allow low ppt detection levels and sub-ppm quantitation levels for mass spectrometric analysis of compounds in a matrix. iFunnel Technology has been incorporated into Agilent Triple Quadrupole and Quadrupole Time-of-Flight (Q-TOF) mass spectrometers to afford low levels of sensitivity and robust operation. Participants in this webinar will discuss the theoretical basis for iFunnel development and design that have allowed its successful use with mass spectrometers. The increased sensitivity directly impacts the detection and quantitation of compounds in diverse application areas including: 1) pharmaceutical research, including metabolic stability, and metabolite ID and profiling, and 2) proteomics, showing the use of increased sensitivity to allow better protein identification and quantitation.
Views: 3237 GENNews
Mass spectroscopy part 6 Ionization in Mass spec
 
16:29
This mass spectrometry tutorial describes different ionization process like matrix assisted laser desoption ionization (MALDI) and electrospray ionization (ESI). For more information, log on to- http://shomusbiology.weebly.com/ Download the study materials here- http://shomusbiology.weebly.com/bio-materials.html
Views: 29207 Shomu's Biology