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MASS SPECTROMETRY

The BYU Chemistry Department uses mass spectrometers to identify molecules. Besides the MS "core" in C270 BNSN, labs also exist in E150, C231, and C354 BNSN. Contact byuchem.proteomics@gmail.com to learn more about BYU's MS facilities.

BYU's biological mass spectrometry facility provides top-tier data acquisition and sample analysis in proteomics (proteins), metablomics, lipidomics, and other omics. The molecules identified are primarily organic, although the ToF-SIMS instrument located in the mass spectrometry core is also used to identify some inorganic molecules.

In particular, the MS facilities at BYU offer instruments for small molecule (molecules weighing <900 Daltons) study and ion mobility study (the Agilent).

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Common Experiment Types
  • Proteomics; identification and quantification
  • Lipidomics; identification, quantification, collision cross-section analysis
  • Small Molecule; identification, quantification, collision cross-section analysis
Agilent LC/Q-ToF
ToF-SIMS
QStar Spectrometer
Orbitrap Spectrometer
GC-MS
FTICR/MS

Agilent 6560 Ion Mobility LC/Q-ToF

The Agilent 6560 Ion Mobility LC/Q-ToF (Agilent) is located in C270 BNSN.

IMS Control Document

The Agilent enables scientific, pharmaceutical, and governmental application. Featuring high-accuracy separation capacity, impressive separation of isobaric classes, thorough characterizations of structures and compounds, and a low-energy drift tube that conserves the structure of gas molecules, the Agilent boosts BYU lab operations.

Policies and Procedures

  1. Use of the Agilent costs $15/hour. All times are rounded up to the nearest 5-minute increment for analyses lasting 60 minutes or less and to the nearest 10 minute increment for analyses longer than 60 minutes.
  2. All sample analyses must be performed by a lab technician.
  3. Samples will not be analyzed unless they are accompanied by a fully completed checklist, which can be downloaded here.
  4. Samples should be prepared according to the methods listed below.
    1. On-Filter Trypsin Digest
    2. In Gel Sample Prep for LCMS Sequencing
  5. If data acquired and/or analyzed by the BYU Agilent is included in a publication, financial support from the Fritz B. Burns Foundation should be acknowledged in the publication. For example: “Mass spectrometry was supported by the Fritz B. Burns Foundation (2016 gift to Brigham Young University).”

ToF-SIMS

The ToF-SIMS is located in C270 BNSN.

A surface-analyzing mass spectrometer, this instrument is used to identify both inorganic and organic molecules. It can even analyze tissue samples, kept cold by two containers of liquid nitrogen.

Use of the ToF-SIMS is granted by request.

QStar Pulsarl Mass Spectrometer

The QStar Pulsarl Mass Spectrometer (QStar) is located in C270 BNSN.

The QStar identifies protein and peptides for biochemists. In addition to utilizing the time-of-flight (ToF) method to separate molecules from one another, the QStar possesses an oMaldi that provides an alternate method of ionization.

Use of the QStar is granted by request.

Orbitrap Fusion Lumos Tribrid Mass Spectrometer

Orbitrap Fusion Lumos Tribrid Mass Spectrometer

The Orbitrap Fusion Lumos Tribrid Mass Spectrometer (Orbitrap) is located in E150 BNSN.

The Orbitrap excels at low-level PTM analyses, multiplexed relative quantitation using isobaric tags, intact protein characterization, and MSn analysis of small molecules. Equipped with bright ion sources, a segmented quadrupole mass filter, advanced vacuum technology, a high-capacity ETD fragmenter, the Advanced Peak Determination (ADP) algorithm for data-dependent experiments, and ultra-high resolution lasers for isobaric compound analysis, the Orbitrap allows for state-of-the-art mass spectrometry.

Policies and Procedures

  1. Use of the Orbitrap costs $15/hour. All times are rounded up to the nearest 5-minute increment for analyses lasting 60 minutes or less and to the nearest 10 minute increment for analyses longer than 60 minutes.
  2. All sample analyses must be performed by a lab technician.
  3. Samples will not be analyzed unless they are accompanied by a fully completed checklist, which can be downloaded here.
  4. Samples should be prepared according to the methods listed below.
    1. On-Filter Trypsin Digest
    2. In Gel Sample Prep for LCMS Sequencing
  5. If data acquired and/or analyzed by the BYU Orbitrap is included in a publication, financial support from the Fritz B. Burns Foundation should be acknowledged in the publication. For example: “Mass spectrometry was supported by the Fritz B. Burns Foundation (2016 gift to Brigham Young University).”

Gas Chromatography-Mass Spectrometer

The Gas Chromatography-Mass Spectrometer (GC-MS) is located in C231 BNSN (Dr. Daniel Austin's lab).

This machine is a combination of two instruments (GC and MS). It uses gas chromatography to separate samples, then uses mass spectrometry to analyze and identify small- and medium-sized molecules.

The GC-MS mostly identifies organic molecules but can also identify small, volatile inorganics, such as the permanent gases, and small inorganic complexes that are not ionic.

Use of the GC-MS is granted by request.

The Tesla FTICR/MS (Fourier Transform Ion Cyclotron Resonance Mass Spectrometer) is located in C354 BNSN (Dr. David Dearden's lab).

Until recently, this instrument had the highest mass-resolving power in the Intermountain West. Fourier transform mass spectrometers serve as electromagnetic "test tubes" in which charged molecules can be trapped and broken apart, revealing their structure, or reacted with neutral gases to reveal their chemistry in unprecedented detail.

This instrument's data acquisition system is currently used to study supramolecular systems (complexes of two or more molecules held together by weak, non-covalent interactions to build larger structures) in the gas phase using experimental and computational methods synergistically.

The Tesla FITCR/MS also develops new techniques specialized for system characterization. The characterization methods being developed as part of this work will not only impact supramolecular mass spectrometry directly, but they will enable applications of supramolecular chemistry that may impact manufacturing, computing, and medicine in the long term.

New experiments use this instrument in conjunction with BYU's National Science Foundation-funded tunable laser facility to probe how molecules trapped and characterized in the FTICR absorb infrared radiation, yielding snapshots revealing how the molecules are folded. This kind of shape information is vital for understanding how molecule-sized machines might function.

The techniques we are developing will also be immediately useful to biomolecular studies. Graduate students will gain valuable training in advanced techniques for high performance mass spectrometry that are vital for the biotechnology industry and the emerging field of proteomics and giving them breadth beyond biochemistry.

Use of the FITCR/MS is granted by request.