Proteomics

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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

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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]

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