<p>Bands from gradient SDS-PAGE (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0002477#pone-0002477-g002" target="_blank">Figure 2</a>) were digested by trypsin and analyzed by mass spectrometry through nano-ESI-MS-MS. For each protein, the following information is indicated: protein name, molecular mass (MW), accession number in NCBInr database, percentage of protein sequence covered by the matched and sequenced tryptic fragments, number of identified peptides out of the total number of tryptic peptides, peptides sequences, mass difference between experimental and theoretical masses, and score (aa, amino acids; expt., expected; calc., calculated).</p
<p>Proteins were purified via VGABA<sub>A</sub>Rα1 or eGFP and identified by LC-MS/MS. Two replicate...
The objective of the work presented in this thesis was to test the concept that tryptic peptides may...
a<p>Assigned spot number as indicated in <a href="http://www.plosone.org/article/info:doi/10.1371/jo...
<p>The sequence coverage of STRA6-GFP based on tryptic peptides identified by LC-MS/MS is shown.</p>...
An enabling capability for proteomics would be the ability to study protein expression on a global s...
<p>GST-PRAME binding proteins were affinity purified as described in Materials & Methods. Bands of a...
<p><sup>1</sup>Score-values calculated by Mascot [Score = −10 × Log (<i>p</i>)] express the probabil...
<p>The most abundant 23 proteins bound to/eluted from the PST affinity column are displayed, as well...
a<p>Spot numbers match those reported in the representative 2-DE images shown in <a href="http://www...
<p>(A) Western analysis of recombinant GBX2 proteins. The amino acid sequences for GBX2 (B) and GBX2...
<p>Sequence coverage of trypsin digested peptide fragments identified. MS/MS spectrum of an identifi...
Affinity purification-mass spectrometry (AP–MS) has become the method of choice for discovering prot...
<p>Certain tryptic peptides were further fragmentated and analyzed by MS-MS to unambiguously identif...
bS Supporting Information Common goals of mass spectrometry (MS)-based proteomicsexperiments are to ...
<p>Spot 8 from <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0017552#pone-00...
<p>Proteins were purified via VGABA<sub>A</sub>Rα1 or eGFP and identified by LC-MS/MS. Two replicate...
The objective of the work presented in this thesis was to test the concept that tryptic peptides may...
a<p>Assigned spot number as indicated in <a href="http://www.plosone.org/article/info:doi/10.1371/jo...
<p>The sequence coverage of STRA6-GFP based on tryptic peptides identified by LC-MS/MS is shown.</p>...
An enabling capability for proteomics would be the ability to study protein expression on a global s...
<p>GST-PRAME binding proteins were affinity purified as described in Materials & Methods. Bands of a...
<p><sup>1</sup>Score-values calculated by Mascot [Score = −10 × Log (<i>p</i>)] express the probabil...
<p>The most abundant 23 proteins bound to/eluted from the PST affinity column are displayed, as well...
a<p>Spot numbers match those reported in the representative 2-DE images shown in <a href="http://www...
<p>(A) Western analysis of recombinant GBX2 proteins. The amino acid sequences for GBX2 (B) and GBX2...
<p>Sequence coverage of trypsin digested peptide fragments identified. MS/MS spectrum of an identifi...
Affinity purification-mass spectrometry (AP–MS) has become the method of choice for discovering prot...
<p>Certain tryptic peptides were further fragmentated and analyzed by MS-MS to unambiguously identif...
bS Supporting Information Common goals of mass spectrometry (MS)-based proteomicsexperiments are to ...
<p>Spot 8 from <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0017552#pone-00...
<p>Proteins were purified via VGABA<sub>A</sub>Rα1 or eGFP and identified by LC-MS/MS. Two replicate...
The objective of the work presented in this thesis was to test the concept that tryptic peptides may...
a<p>Assigned spot number as indicated in <a href="http://www.plosone.org/article/info:doi/10.1371/jo...