Proteomics

Dataset Information

0

Mass spectrometry data of the ERα-NTD samples exposed to 0-50ms x-ray beam


ABSTRACT: Here we present MS data of ERα-NTD protein samples exposed to 0-50 ms of X-ray beam at the Advanced Light Source (Berkeley, CA). Irradiated protein samples were digested with two sets of proteases, Asp-N and Lys-C, and pepsin. LC-MS/MS data was utilized to identify 16 sites of modification listed in table S3. LC-MS data were used to quantify the extent of oxidative modifications for these 16 residues. Quantification of oxidative modification for all sites has been done manually.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Janna Kiselar  

LAB HEAD: Janna Kiselar

PROVIDER: PXD011361 | Pride | 2020-05-26

REPOSITORIES: pride

Dataset's files

Source:
Action DRS
F050342.mgf Mgf
F050342.pride.mgf.gz Mgf
F050345.mzid.gz Mzid
F050345.pride.mztab.gz Mztab
NTD_WT.fasta Fasta
Items per page:
1 - 5 of 21
altmetric image

Publications


The N-terminal transactivation domain (NTD) of estrogen receptor alpha, a well-known member of the family of intrinsically disordered proteins, mediates the receptor's transactivation function. However, an accurate molecular dissection of NTD's structure-function relationships remains elusive. Here, we show that the NTD adopts a mostly disordered, unexpectedly compact conformation that undergoes structural expansion on chemical denaturation. By combining small-angle X-ray scattering, hydroxyl ra  ...[more]

Similar Datasets

2014-03-02 | E-GEOD-53533 | biostudies-arrayexpress
2014-03-03 | E-GEOD-53532 | biostudies-arrayexpress
| PRJNA889874 | ENA
2012-03-23 | E-GEOD-34013 | biostudies-arrayexpress
2013-07-05 | E-GEOD-42349 | biostudies-arrayexpress
2013-06-11 | E-GEOD-20187 | biostudies-arrayexpress
2012-09-30 | E-GEOD-34188 | biostudies-arrayexpress
2016-09-27 | PXD003208 | Pride
2023-03-13 | PXD037438 | Pride
2019-03-04 | PXD009875 | Pride