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

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A90043%2F20%3A00139211" target="_blank" >RIV/00216224:90043/20:00139211 - isvavai.cz</a>

Alternative codes found

RIV/61388971:_____/20:00531921 RIV/00216208:11310/20:10413326

Result on the web

<a href="https://www.sciencedirect.com/science/article/pii/S1874391920300841?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S1874391920300841?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.jprot.2020.103716" target="_blank" >10.1016/j.jprot.2020.103716</a>

Result language

angličtina

Original language name

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

Original language description

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.

Czech name

—

Czech description

—

Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10609 - Biochemical research methods

Project

—

Continuities

—

Publication year

2020

Confidentiality

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

Name of the periodical

Journal of Proteomics

ISSN

1874-3919

e-ISSN

—

Volume of the periodical

218

Issue of the periodical within the volume

apr

Country of publishing house

NL - THE KINGDOM OF THE NETHERLANDS

Number of pages

7

Pages from-to

1-7

UT code for WoS article

000527377400004

EID of the result in the Scopus database

2-s2.0-85080076655