Hydroxyl radical footprinting analysis of a human haptoglobin-hemoglobin complex

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F22%3A00553501" target="_blank" >RIV/61388971:_____/22:00553501 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11310/22:10454373

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S1570963921001412?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S1570963921001412?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bbapap.2021.140735" target="_blank" >10.1016/j.bbapap.2021.140735</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Hydroxyl radical footprinting analysis of a human haptoglobin-hemoglobin complex

Popis výsledku v původním jazyce

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. FPOP footprinting using a timsTOF Pro mass spectrometer revealed 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 complex formation were Met76 and Tyr140 in Hba, and Tyr280 and Trp284 in Hp beta. 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 beta Trp37 and Hp beta Phe292 was not confirmed by our data. Data are available via ProteomeXchange with identifier PXD021621.

Název v anglickém jazyce

Hydroxyl radical footprinting analysis of a human haptoglobin-hemoglobin complex

Popis výsledku anglicky

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. FPOP footprinting using a timsTOF Pro mass spectrometer revealed 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 complex formation were Met76 and Tyr140 in Hba, and Tyr280 and Trp284 in Hp beta. 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 beta Trp37 and Hp beta Phe292 was not confirmed by our data. Data are available via ProteomeXchange with identifier PXD021621.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2022

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Biochimica Et Biophysica Acta-Proteins and Proteomics

ISSN

1570-9639

e-ISSN

1878-1454

Svazek periodika

1870

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

6

Strana od-do

140735

Kód UT WoS článku

000721689400001

EID výsledku v databázi Scopus

2-s2.0-85119185232