| # |
GPM |
# proteins |
Description |
|
1. |
GPM77710002411
peptide
model
gel
aaa
go
mh
|
886 |
- BRENDA cell culture: none
- BRENDA tissue: none
- CELL cell type: none
- GO subcellular: GO:0005623
 - email: shuang@jcvi.org
- institution: J. Craig Venter Institute
- name: Rembert Pieper, Srilatha Kuntumalla, Shih-Ting Huang
- project: Sample 1: Shigella dysenteriae analyzed by 2D LC-MS/MS
- project comment: Peptidome PSM1302, MudPit run PSM1302_2DLCSd090514. The sample preparation procedure started with the extraction of soluble proteins from whole cell lysates of S. dysenteriae samples. The extracted proteins were subjected to double trypsin digestion. Tryptic peptide mixtures were separated using SCX liquid chromatography (1st dimension) and C18 (2nd dimension) and analyzed by ESI-MS/MS.
|
|
2. |
GPM77710002455
peptide
model
gel
aaa
go
mh
|
890 |
- BRENDA cell culture: none
- BRENDA tissue: none
- CELL cell type: none
- GO subcellular: GO:0005623
 - email: shuang@jcvi.org
- institution: J. Craig Venter Institute
- name: Rembert Pieper, Srilatha Kuntumalla, Shih-Ting Huang
- project: Sample 1: Shigella dysenteriae analyzed by 2D LC-MS/MS
- project comment: Peptidome PSM1302, MudPit run PSM1302_2DLCSd090518. The sample preparation procedure started with the extraction of soluble proteins from whole cell lysates of S. dysenteriae samples. The extracted proteins were subjected to double trypsin digestion. Tryptic peptide mixtures were separated using SCX liquid chromatography (1st dimension) and C18 (2nd dimension) and analyzed by ESI-MS/MS.
|
|
3. |
GPM77710002486
peptide
model
gel
aaa
go
mh
|
933 |
- BRENDA cell culture: none
- BRENDA tissue: none
- CELL cell type: none
- GO subcellular: GO:0005623
 - email: shuang@jcvi.org
- institution: J. Craig Venter Institute
- name: Rembert Pieper, Srilatha Kuntumalla, Shih-Ting Huang
- project: Sample 1: Shigella dysenteriae analyzed by 2D LC-MS/MS
- project comment: Peptidome PSM1302, MudPit run PSM1302_2DLCSd090522. The sample preparation procedure started with the extraction of soluble proteins from whole cell lysates of S. dysenteriae samples. The extracted proteins were subjected to double trypsin digestion. Tryptic peptide mixtures were separated using SCX liquid chromatography (1st dimension) and C18 (2nd dimension) and analyzed by ESI-MS/MS.
|