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Networking
Education
Information Exchange |
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"Mass Spectrometric Approaches to Proteomics"
PRESENTATION ABSTRACTS
Thursday November 15, 2001
South San Francisco, CA USA
Exelixis, Inc.
click
here for presentation bios
click
here for poster abstracts
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| Title |
Abstract |
TUTORIAL
"Current Mass Spectrometric Approaches to Proteomics" by
Kamala
Tyagarjan Lynx Therapeutics kamala@lynxgen.com
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There is no abstract for this very informative tutorial,
but Dr. Tyagarjan is graciously allowing the posting of
the entire contents on the site, following the meeting.
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"Isotope-coded Affinity Tag (ICAT) technology for
Quantitative Protein Expression Analysis: Advances and
Challenges" by Lydia
Nuwaysir
Applied Biosystems|MDS Sciex nuwayslm@appliedbiosystems.com |
Quantitative
protein expression profiling by Isotope-coded Affinity
Tag (ICAT>TM)
labeling is an exciting new alternative to similar
experiments using
2-D gel technology. This technique is much more amenable
to automation
than 2-D gel analysis and imaging and offers the
advantages of looking at membrane proteins as
well as low abundance proteins. However,
this technology has its own limitations such as being
cysteine specific.
In addition, high quality quantitation (C.V s less than
20%) from
LC/MS/MS data, where the peptide pairs do not entirely
coelute, has its
challenges. This talk will cover an overview of ICAT
technology and focus
on several issues involved with processing this data,
and its implications
on experimental design. |
"Development of High Throughput Proteomic Analysis of Proteins Separated by Gel Electrophoresis using MALDI
TOF/TOF MS" by Lan
Huang, UCSF lan@cgl.ucsf.edu
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We
are developing a methodology for
high throughput proteomic analysis
of gel-separated
proteins, using robotic sample
preparation techniques, a novel
MALDI-TOF/TOF tandem mass
spectrometer, and automated data
collection and
analysis with feedback control of
the experiment. This
high throughput approach has been
employed for comprehensive identification
of interacting proteins at
large scale. Here, protein
interactions were sampled
using immobilized nucleoporins. The
nucleoporin interacting proteins
were identified using peptide mass
mapping and peptide sequencing
with automated
database searching. The results have
provided a basis for
our great understanding of the
transport mechanism. Meanwhile,
MALDI TOF/TOF mass
spectrometer has established its
ability to generate excellent
quality of
high energy CID spectra with low
fmol sensitivity and with sufficient
speed for high
throughput analysis. Furthermore,
most spectra were of sufficient
quality to be suitable for de novo
peptide sequencing, essential
for dealing with unknown proteins or
peptide sequences inconsistent
with databases that were resulted
from genomic sequence errors,
differences in DNA splicing,
chemical modifications or
unpredicted enzyme
cleavages. |
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