Editing GPM32100023441

Views

From TheGPMWiki

Warning: You are not logged in. Your IP address will be recorded in this page's edit history.

The edit can be undone. Please check the comparison below to verify that this is what you want to do, and then save the changes below to finish undoing the edit.

This data was obtained from the PNNL database and it is supporting material for: Applying a Targeted Label-Free Approach Using LC-MS AMT Tags to Evaluate Changes in Protein Phosphorylation Following Phosphatase Inhibition. Feng Yang, N Jaitly, H Jayachandran, Q Luo, ME Monroe, X Du, MA Gritsenko, R Zhang, DJ Anderson, SO Purvine, JN Adkins, RJ Moore, HM Mottaz, SJ Ding, MS Lipton, DG Camp, HR Udseth, RD Smith, and S Rossie. Journal of Proteome Research; (2007) 6, 4489-4497. The data can be found
[http://gpmdb.thegpm.org/thegpm-cgi/plist.pl?path=/gpm/archive/321/GPM32100023441.xml&proex=-1 here].

==Experimental Details==

The data was acquired using an LTQ instrument. Phosphorylated peptides were enriched by first methylating the carboxyl groups in the peptides and then using an immobilized metal ion column.

==Comments==

The data is of good quality. It consists almost entirely of phosphopeptides. It also contains a significant number of peptide assignments that have not been previously observed. The observed proteins are predominantly nuclear and cytoplasmic.

Please note that all contributions to TheGPMWiki may be edited, altered, or removed by other contributors. If you do not want your writing to be edited mercilessly, then do not submit it here.
You are also promising us that you wrote this yourself, or copied it from a public domain or similar free resource (see TheGPMWiki:Copyrights for details). Do not submit copyrighted work without permission!

Summary:

Cancel | Editing help (opens in new window)

Retrieved from "http://wiki.thegpm.org/wiki/GPM32100023441"

Editing GPM32100023441

Views

Navigation

Search

Toolbox

Personal tools

@@ Line 4: / Line 4: @@
 ==Experimental Details==
-The data was acquired using an LTQ instrument. Phosphorylated peptides were enriched by first methylating the carboxyl groups in the peptides and then using an immobilized metal ion column. The peptide-to-spectrum assignments were made assuming methyl groups on all aspartic and glutamic acids, as well as all peptide C-termini. Phosphoryl groups were allowed as a possibility on serine, threonine and tyrosine residues.
+The data was acquired using an LTQ instrument. Phosphorylated peptides were enriched by first methylating the carboxyl groups in the peptides and then using an immobilized metal ion column.
 ==Comments==
 The data is of good quality. It consists almost entirely of phosphopeptides. It also contains a significant number of peptide assignments that have not been previously observed. The observed proteins are predominantly nuclear and cytoplasmic.