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Keck
Home Page > New Services in the Keck Facility
New Services in the Keck Facility
This new protein profiling service allows researchers to multiplex four samples,
providing both identification and quantitation on hundreds to proteins
simultaneously.
Opened February
1, 2002 and is now providing all services to both
Yale and non-Yale investigators.
When coupled with HPLC size exclusion chromatography (SEC), laser light scattering (LS)
provides the unique capability of determining the absolute molecular weights of proteins
and their protein:protein complexes.
More information about
the service in Laser Light Scattering Determination of
Native Protein Molecular Weights.
High resolution and high
mass accuracy Fourier transform ion
cyclotron resonance (FT-ICR) mass spectrometer
FT-ICR MS
offers the highest mass resolving power and highest mass accuracy out of all
mass spectrometer types and is ideal for analysis of complex biological sample
mixtures. The instrument is used to identify proteins from accurate mass of
tryptic digests, to elucidate posttranslational modifications (PTM) of
proteins/peptides, to determine exact mass on small molecules, to determine
accurate mass of proteins and/or protein mixture, to provide comparative protein
profiles in two different proteomes, and to de novo sequence peptides and
proteins. When internally calibrated all exact mass measurement accuracies
typically fall <2 ppm (parts per million), and all peptide masses, when
calibrated externally, used for protein identification fall within <3ppm.
Our
9.4 Tesla Bruker Apex Qe FTMS "Combi"
system is equipped with a combination of Matrix assisted laser desorption
ionization [MALDI] and conventional and as well as nano Electrospray ionization
[ESI] sources. Multiple fragmentation techniques (Collision induced dissociation
[CID, MSn], Infrared multiphoton dissociation [IRMPD], and Electron captured
dissociation [ECD]) can be selected to enhance determination of post
translationally modified sites both in peptides and intact proteins. Contrary to
popular belief, the use of various forms of hyphenated techniques (LC-MS,
2DLC-MS, LC-MS/MS, etc.) are now possible with this platform. These various
features and the technical capabilities of the FTMS system expand its use for a
variety of proteomics applications. Please see detail description of the current
services offered with our FTMS system.
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