Voyager de str spectrometer

Manufactured by Thermo Fisher Scientific

The Voyager-DE STR spectrometer is a mass spectrometry instrument designed for matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) analysis. It is capable of accurately measuring the mass-to-charge ratios of ionized molecules, providing detailed information about the composition and structure of a wide range of samples.

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Lab products found in correlation

Nanodrop 2000, by Thermo Fisher Scientific (2 mentions) Lct premier, by Waters Corporation (1 mentions) Acquity lc, by Waters Corporation (1 mentions) Vxr 500 spectrometer, by Agilent Technologies (1 mentions) Micromass q tof spectrometer, by Thermo Fisher Scientific (1 mentions) Breeze 2, by Waters Corporation (1 mentions)

3 protocols using voyager de str spectrometer

Spectroscopic Characterization Techniques

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NMR spectra were
obtained on Bruker
AV 500 and DRX 500 MHz spectrometers. ¹H NMR spectra were
acquired with a relaxation delay of 2 s for small molecules and 30
s for polymers. UV–vis spectroscopy was performed using a Biomate
5 Thermo Spectronic spectrometer or Thermo Scientific NanoDrop 2000
(for small quantities). ESI-MS data were gathered on a Waters LCT
premier with ACQUITY LC. Infrared absorption spectra were recorded
using a PerkinElmer FT-IR equipped with an ATR accessory. Photoreactions
were carried out in a photochemical safety cabinet equipped with a
broadband, medium pressure Ace-Hanocia 7825–34 quartz mercury
arc lamp and ACE Glass Inc. power supply. Matrix-assisted laser desorption/ionization
time-of-flight mass (MALDI-TOF MS) spectrometry data was gathered
using sinapic acid (SA) as a matrix on an Applied Biosystems Voyager-DE-STR
spectrometer.

Lin E.W., Boehnke N, & Maynard H.D. (2014). Protein–Polymer Conjugation via Ligand Affinity and Photoactivation of Glutathione S-Transferase. Bioconjugate Chemistry, 25(10), 1902-1909.

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Characterization of Hyperbranched Polymers

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Mass spectral analysis was performed using ESI on a Waters Micromass Q-Tof spectrometer or MALDI-TOF on an Applied Biosystems Voyager-DE STR spectrometer. Nuclear magnetic resonance (NMR) spectra were recorded on a Varian U400, UI400, U500 or VXR500 spectrometer. Additionally, the molecular weights of HPGs were evaluated by gel permeation chromatography (GPC, Waters Breeze 2) with a Styragel HT column. 20 mM LiBr in N,N-dimethylformamide (DMF) was used as an eluent. Values were based on calibration against polyethylene glycol (PEG) standards.

Smith C.E., Ernenwein D., Shkumatov A., Clay N., Lee J., Melhem M., Misra S., Zimmerman S.C, & Kong H. (2015). Hydrophilic Packaging of Iron Oxide Nanoclusters for Highly Sensitive Imaging. Biomaterials, 69, 184-190.

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Characterizing Protein C-terminus Amidation

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Positive ion MALDI-TOF mass spectrometry was carried out on an Applied Biosystems Voyager-DE STR spectrometer using a α–cyano–4–hydroxycinnamic acid matrix. Amidation of the C-terminus was determined by the difference between the calculated and experimental molecular mass and confirmed by nanoNMR spectroscopy.

Franco A., Dovell S., Moller C., Grandal M., Clark E, & Marí F. (2018). Structural Plasticity of Mini-M Conotoxins: Expression of all mini-M subtypes by Conus regius. The FEBS journal, 285(5), 887-902.

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