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  Magnetite-binding proteins from the magnetotactic bacterium Desulfamplus magnetovallimortis BW-1

Pohl, A., Young, S., Schmitz, T. C., Farhadi, D., Zarivach, R., Faivre, D., et al. (2021). Magnetite-binding proteins from the magnetotactic bacterium Desulfamplus magnetovallimortis BW-1. Nanoscale, 13(48), 20396-20400. doi:10.1039/D1NR04870H.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0009-96AD-B Version Permalink: https://hdl.handle.net/21.11116/0000-000B-06BA-D
Genre: Journal Article

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 Creators:
Pohl, Anna1, Author           
Young, Sarah2, Author           
Schmitz, Tara C.3, Author
Farhadi, Daniel3, Author           
Zarivach, Raz, Author
Faivre, Damien1, Author           
Blank, Kerstin G.3, Author           
Affiliations:
1Damien Faivre, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863290              
2Amaia Cipitria, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_2489692              
3Kerstin Blank, Mechano(bio)chemie, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_2301698              

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 Abstract: Magnetite-binding proteins are in high demand for the functionalization of magnetic nanoparticles. Binding analysis of six previously uncharacterized proteins from the magnetotactic Deltaproteobacterium Desulfamplus magnetovallimortis BW-1 identified two new magnetite-binding proteins (Mad10, Mad11). These proteins can be utilized as affinity tags for the immobilization of recombinant fusion proteins to magnetite.

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Language(s): eng - English
 Dates: 2021-11-252021
 Publication Status: Issued
 Pages: -
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 Rev. Type: -
 Identifiers: DOI: 10.1039/D1NR04870H
BibTex Citekey: D1NR04870H
Other: https://doi.org/10.5281/zenodo.5735990
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Title: Nanoscale
  Abbreviation : Nanoscale
Source Genre: Journal
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Publ. Info: Cambridge, UK : Royal Society of Chemistry
Pages: - Volume / Issue: 13 (48) Sequence Number: - Start / End Page: 20396 - 20400 Identifier: ISSN: 2040-3364