Influence of cross-linker polarity on selectivity towards
lysine side chains

J 2020

Influence of cross-linker polarity on selectivity towards lysine side chains

FIALA, Jan; Zdenek KUKACKA a Petr NOVAK

Základní údaje

Originální název

Influence of cross-linker polarity on selectivity towards lysine side chains

Autoři

FIALA, Jan; Zdenek KUKACKA a Petr NOVAK

Vydání

Journal of Proteomics, Amsterdam, Elsevier Science, 2020, 1874-3919

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10609 Biochemical research methods

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 4.044

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:90043/20:00139211

Organizační jednotka

CIISB

Klíčová slova anglicky

Structural mass spectrometry; Protein structure; Chemical cross-linking; Disuccinimidyl glutarate; Bis(sulfosuccinimidyl) glutarate; Bovine serum albumin

Štítky

ne MU, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 28. 3. 2025 18:02, Mgr. Eva Dubská

Anotace

V originále

The combination of chemical cross-linking and mass spectrometry is currently a progressive technology for deriving structural information of proteins and protein complexes. In addition, chemical cross-linking is a powerful tool for stabilizing macromolecular complexes for single particle cryo-electron microscopy. Broad pallets of cross-linking chemistry, currently available for the majority of cross-linking experiments, still rely on the amine-reactive N-hydroxysuccinimide esters targeting mainly N-termini and lysine side chains. These cross-linkers are divided into two groups: water soluble and water insoluble; and research teams prefer one or another speculating on the benefits of their choice. However, the effect of cross-linker polarity on the outcome of cross-linking reaction has never been studied. Herein, we use both polar (bis(sulfosuccinimidyl) glutarate) and nonpolar (disuccinimidyl glutarate) cross-linkers and systematically investigated the impact of cross-linker hydrophobicity on resulting distance constraints, using bovine serum albumin as a model protein.

Návaznosti

90043, velká výzkumná infrastruktura

Název: CIISB

Citovat

FIALA, Jan; Zdenek KUKACKA a Petr NOVAK. Influence of cross-linker polarity on selectivity towards lysine side chains. Journal of Proteomics. Amsterdam: Elsevier Science, 2020, roč. 218, apr, s. 1-7. ISSN 1874-3919. Dostupné z: https://doi.org/10.1016/j.jprot.2020.103716.

@article{2487301,
   author = {Fiala, Jan and Kukacka, Zdenek and Novak, Petr},
   article_location = {Amsterdam},
   article_number = {apr},
   doi = {https://doi.org/10.1016/j.jprot.2020.103716},
   keywords = {Structural mass spectrometry; Protein structure; Chemical cross-linking; Disuccinimidyl glutarate; Bis(sulfosuccinimidyl) glutarate; Bovine serum albumin},
   language = {eng},
   issn = {1874-3919},
   journal = {Journal of Proteomics},
   title = {Influence of cross-linker polarity on selectivity towards lysine side chains},
   url = {https://www.sciencedirect.com/science/article/pii/S1874391920300841?via%3Dihub},
   volume = {218},
   year = {2020}
}

TY  - JOUR
ID  - 2487301
AU  - Fiala, Jan - Kukacka, Zdenek - Novak, Petr
PY  - 2020
TI  - Influence of cross-linker polarity on selectivity towards lysine side chains
JF  - Journal of Proteomics
VL  - 218
IS  - apr
SP  - 1-7
EP  - 1-7
PB  - Elsevier Science
SN  - 18743919
KW  - Structural mass spectrometry
KW  - Protein structure
KW  - Chemical cross-linking
KW  - Disuccinimidyl glutarate
KW  - Bis(sulfosuccinimidyl) glutarate
KW  - Bovine serum albumin
UR  - https://www.sciencedirect.com/science/article/pii/S1874391920300841?via%3Dihub
N2  - The combination of chemical cross-linking and mass spectrometry is currently a progressive technology for deriving structural information of proteins and protein complexes. In addition, chemical cross-linking is a powerful tool for stabilizing macromolecular complexes for single particle cryo-electron microscopy. Broad pallets of cross-linking chemistry, currently available for the majority of cross-linking experiments, still rely on the amine-reactive N-hydroxysuccinimide esters targeting mainly N-termini and lysine side chains. These cross-linkers are divided into two groups: water soluble and water insoluble; and research teams prefer one or another speculating on the benefits of their choice. However, the effect of cross-linker polarity on the outcome of cross-linking reaction has never been studied. Herein, we use both polar (bis(sulfosuccinimidyl) glutarate) and nonpolar (disuccinimidyl glutarate) cross-linkers and systematically investigated the impact of cross-linker hydrophobicity on resulting distance constraints, using bovine serum albumin as a model protein.
ER  -

FIALA, Jan; Zdenek KUKACKA a Petr NOVAK. Influence of cross-linker polarity on selectivity towards lysine side chains. \textit{Journal of Proteomics}. Amsterdam: Elsevier Science, 2020, roč.~218, apr, s.~1-7. ISSN~1874-3919. Dostupné z: https://doi.org/10.1016/j.jprot.2020.103716.

Přehled o publikaci