All reactions involving air or moisture sensitive reagents were carried out in flame-dried glassware under an atmosphere of argon. All solvents and reagents were purified according to standard procedures or were used as-received from Sigma Aldrich, Acros, Alfa Aesar, or TCI Europe. Mass spectra were recorded on a Finnigan MAT 4200S, a Bruker Daltonics Micro Tof, and a Waters-Micromass Quattro LCZ (ESI) and peaks are given in m/z (% of basis peak). ESI-MS (m/z) and HRMS (m/z) were performed using a Bruker MicroTof (loop injection; resolution: 10 000), a LTQ Orbitrap XL (nanospray inlet, 1.1 kV, resolution: 30 000), and an Autoflex Speed TOF-MS (Bruker Daltonics). MALDI spectra were recorded with an Autoflex Speed TOF-MS (Bruker Daltonics) in linear mode. GC-MS (EI, 70 eV) was performed on a combined setup of an Agilent 6890N chromatograph equipped with a HP-5 column, using helium (∼1 bar) as the carrier gas, and a Waters Micromass Quattro Micro spectrometer. Gas chromatography (GC-FID) was performed on an Agilent 7890A chromatograph, which was equipped with a HP-5 column (30 m × 0.32 mm, film thickness 0.25 μm), using H2 (∼1 bar) as the carrier gas.
Autoflex speed tof ms
Manufactured by Bruker
The Autoflex Speed TOF-MS is a time-of-flight mass spectrometer manufactured by Bruker. The core function of this instrument is to analyze the mass-to-charge ratio of ionized molecules or particles, providing information about their molecular composition.
Automatically generated - may contain errors
Lab products found in correlation
2 protocols using autoflex speed tof ms
1
Air- and Moisture-Sensitive Reactions
2
MALDI-TOF/TOF Analysis of Pin1 Modifications
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An Autoflex
Speed TOF MS or an Ultraflextreme TOF/TOF MS (Bruker
Daltonics), both equipped with a Nd:YAG (solid state) laser operating
at 355 nm, were used to obtain spectra. All spectra were obtained
in positive ion mode. Peptide-CHCA solutions (1 μL) were deposited
on 384-spot MALDI target plates and air-dried prior to analysis. Full
mass spectra of peptides were obtained in reflectron mode on the Ultraflextreme,
using a 500–4500 mass range. Spectra from treated and untreated
samples were overlaid to identify peaks corresponding to masses appearing
in spectra from ONE-treated Pin1 samples which did not appear in unmodified
Pin1 samples. Selected peptide ions were dissociated using LIFT on
the TOF/TOF. TOF/TOF fragmentation data were interrogated using FlexAnalysis
software and analyzed against a theoretical Pin1 peptide digest using
Protein Prospector.
Speed TOF MS or an Ultraflextreme TOF/TOF MS (Bruker
Daltonics), both equipped with a Nd:YAG (solid state) laser operating
at 355 nm, were used to obtain spectra. All spectra were obtained
in positive ion mode. Peptide-CHCA solutions (1 μL) were deposited
on 384-spot MALDI target plates and air-dried prior to analysis. Full
mass spectra of peptides were obtained in reflectron mode on the Ultraflextreme,
using a 500–4500 mass range. Spectra from treated and untreated
samples were overlaid to identify peaks corresponding to masses appearing
in spectra from ONE-treated Pin1 samples which did not appear in unmodified
Pin1 samples. Selected peptide ions were dissociated using LIFT on
the TOF/TOF. TOF/TOF fragmentation data were interrogated using FlexAnalysis
software and analyzed against a theoretical Pin1 peptide digest using
Protein Prospector.
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