Proteomics

Dataset Information

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Hydroxyl radical footprinting analysis of a human haptoglobin-hemoglobin complex


ABSTRACT: Methods of structural mass spectrometry have become more popular to study protein structure and dynamics. Among them, fast photochemical oxidation of proteins (FPOP) has several advantages such as irreversibility of modifications and more facile determination of the site of modification with single residue resolution. In the present study, FPOP analysis was applied to study the hemoglobin (Hb) – haptoglobin (Hp) complex allowing identification of respective regions altered upon the complex formation. The footprinting using a timsTOF Pro mass spectrometer allowed to obtain structural information for 84 and 76 residues in Hp and Hb, respectively, including statistically significant differences in the modification extent below 0.3 %. The most affected residues upon the complex formation were Met76 and Tyr140 in Hbα, and Tyr280 and Trp284 in Hpβ. The data allowed determination of amino acids directly involved in Hb – Hp interactions and those located outside of the interaction interface yet affected by the complex formation. Also, previously modeled interaction between Hb βTrp37 and Hp βPhe292 was not confirmed by our data.

INSTRUMENT(S): timsTOF Pro

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Dmitry Loginov  

LAB HEAD: Petr Novak

PROVIDER: PXD021621 | Pride | 2021-12-30

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
HbHp_ctrl.csv Csv
HbHp_laser.csv Csv
HbHp_rawdata.zip Other
Hb_ctrl.csv Csv
Hb_laser.csv Csv
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Publications

Hydroxyl radical footprinting analysis of a human haptoglobin-hemoglobin complex.

Loginov Dmitry S DS   Fiala Jan J   Brechlin Peter P   Kruppa Gary G   Novak Petr P  

Biochimica et biophysica acta. Proteins and proteomics 20211103 2


Methods of structural mass spectrometry have become more popular to study protein structure and dynamics. Among them, fast photochemical oxidation of proteins (FPOP) has several advantages such as irreversibility of modifications and more facile determination of the site of modification with single residue resolution. In the present study, FPOP analysis was applied to study the hemoglobin (Hb) - haptoglobin (Hp) complex allowing identification of respective regions altered upon the complex forma  ...[more]

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