| Thermo has obtained an exclusive license for
Electron Transfer Dissociation (ETD) technology from the University
of Virginia. ETD is an innovative new ion fragmentation technology
that provides sequence information not available from conventional
methods currently used on ion trap mass spectrometers. "ETD will
help shed new light on many important, unanswered questions in
contemporary biology,” said Dr. Don Hunt, principal investigator at
the University of Virginia. “ETD represents a landmark advance in
the field of proteomics. This new methodology is a powerful and
reliable analytical solution for protein
characterization." |
| ETD - A New Era in
Structural Information for Proteomics |
|
Thermo's new ETD option
for the LTQ XL™ mass spectrometer represents the first product
to use ETD ion chemistry, as licensed from the University of
Virginia and developed by Professor Don Hunt:
- ECD-like
fragmentation with an ion trap
- Available for the new LTQ
XL linear ion trap
- Powerful new method for
phosphorylation analysis
- N- and O-linked carbohydrate
analysis
- Use with CID and PQD for best possible protein
coverage |
| Learn More About
ETD Now |
| Webinar: Advancing
Proteomics with Ion/Ion Chemistry - ETD and
Beyond |
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In this recorded
webinar Dr. Joshua Coon, Assistant Professor, Departments of
Chemistry and Biomolecular Chemistry, University of
Wisconsin-Madison presents a novel technique combining ETD and
CAD using the Finnigan™ LTQ™ and the TriVersa NanoMate
(Advion) to achieve greater sequence coverage of
proteins. |
| View Webinar
Recording Now |
| Proteomics: Analysis
of Mouse Urinary Proteins using ETD and CID - A Combined
Strategy |
|
| The analysis of intact
proteins can provide complete sequence coverage, including
site-specific modifications or mutations, information which is
difficult to obtain at the peptide level. ECD has been applied
in top-down proteomics, with successful applications reported
for large peptides and intact proteins. However, intact
protein ion dissociation efficiency is significantly lower
than that of peptides, and implementation of ECD is limited to
FT-ICR instruments. A novel fragmentation method, electron
transfer dissociation (ETD) shows ECD-like polypeptide
fragmentation patterns, and has been implemented on the
Finnigan LTQ linear ion trap. |
 |
| Download Full
Article [PDF 680 kB] |
| Quantum Waves: The
Impact of "Reversed Energy Ramp" on Metabolite
Identification |
|
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The Reversed
Energy Ramp (RER) scan function linearly reduces the amount of
collision voltage (energy), while the product ions are scanned
from low to high mass. This scan function enables the creation
of fragments with Normalized Collision Energy™ which in turn
results in more efficient creation of product ions. The RER
scan thus coupled with the Constant Neutral Loss (CNL) and
Precursor ion Scan (PS) on a Finnigan TSQ™ Quantum mass
spectrometer is a powerful tool for metabolite
identification. |
| Download Full
Article [PDF 337 kB] |
| Software: PEAKS
Studio 4.0 for de novo sequencing |
|
PEAKS is an elegant
software solution for peptide sequencing and protein
identification from tandem mass spectrometry (MS/MS) data.
PEAKS Studio 4.0 the latest version of the PEAKS de
novo sequencing software by Bioinformatics Solutions of
Waterloo, Ontario (Canada). Users of Finnigan LTQ FT™ and LTQ
Orbitrap would benefit using PEAKS Studio 4.0 as a complement
to the SEQUEST®-based protein identification in BioWorks. The
software package allows for automatic or manual de novo
sequencing and is a very fast algorithm, sequencing at
approximately 1 second per spectrum.
*SEQUEST
is a registered trademark of the University of
Washington |
 |
| Learn
More |
| ASMS
Posters and Presentations CD |
|
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This information
packed CD contains Thermo's posters and presentations from
ASMS 2006 covering topics involving metabolism, quantitation
and proteomics. Learn more about the latest techniques in mass
spectrometry and chromatography including FAIMS, ETD, H-SRM
and the latest in application software. |
| Order
Now |
| CoSMoS 2006 - View
Program Agenda |
|
| The Conference on Small
Molecule Science addresses the latest in small molecule
science topics in a unique, intimate setting. This innovative
research-style meeting promotes high-level discussions
focusing on the exchange of practical experience and ideas,
academic research and novel techniques. |
 |
| View
Agenda |
| Thermo at IMSC 2006 -
Prague Congress Centre, Prague, Czech
Republic |
|
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Thermo is pleased
to present its full range of state-of-the-art instrument
systems, advanced software, and innovative column technology
at IMSC 2006. Learn more from our experts about the latest
cutting edge developments in instrumentation - ion trap,
quadrupole, hybrid, magnetic sector mass spectrometers, and
hyphenated multi-instrument combinations of
products.
Watch this space for further
information. |
| |
| The NEW LTQ FT Ultra
Product Brochure |
|
| The LTQ FT Ultra mass
spectrometer from Thermo Electron is the next generation
hybrid FTICR featuring a novel ICR cell design, the Ultra
Cell. This cell design produces enhanced sensitivity and
greater dynamic range. The linear excitation characteristics
of the cell allow larger cyclotron radii which significantly
reduces space charge effects. These performance gains are
achieved without the costs and difficulties associated with a
higher field magnet. |
 |
| Download Brochure
[PDF 1374 kB] |
| Trap
Talk: High Resolution Isolation |
|
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MSn analysis of
ions in an ion trap mass spectrometer is a differentiating
technique for the structural identification of a wide variety
of compounds. The simplest approach involves, isolating ions
with a specific m/z value of interest, energetically
exciting these ions, generating fragment ions through
collisions with a buffer gas, and performing mass analysis of
the fragments produced. The isolation step is critical to the
process since... |
| Download Full
Article [PDF 162
kB] |
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