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Mass Spectrometry Reveals the Assembly Pathway of Encapsulated Ferritins and Highlights a Dynamic Ferroxidase Interface

27 September 2019, Version 1
Working Paper
This content is an early or alternative research output and has not been peer-reviewed by Cambridge University Press at the time of posting.

Abstract

Encapsulated ferritins (EncFtn) are a recently characterised member of the ferritin superfamily. EncFtn proteins are sequestered within encapsulin nanocompartments and form a unique biological iron storage system. Here, we use native mass spectrometry and hydrogen-deuterium exchange mass spectrometry to elucidate the metal-mediated assembly pathway of EncFtn.

Keywords

Encapsulin Nanocompartments
ferritin
mass spectrometry
Native Mass Spectrometry Characterization
HDX MS
protein assembly mechanisms
Protein Structure

Supplementary materials

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Ross et al Assembly Pathway SI (ChemRxiv)
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Now Published

Mass spectrometry reveals the assembly pathway of encapsulated ferritins and highlights a dynamic ferroxidase interface [opens in a new tab]
Jennifer Ross, Thomas Lambert, Cecilia Piergentili, Didi He, Kevin J. Waldron, C. Logan Mackay, Jon Marles-Wright, David J. Clarke journal article
Chemical Communications , Volume 56, Issue 23
Online publication date: 2020

Version History

Sep 27, 2019 Version 1

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The content is available under CC BY NC ND 4.0 [opens in a new tab]

DOI

10.26434/chemrxiv.9901346.v1
D O I: 10.26434/chemrxiv.9901346.v1 [opens in a new tab]

Funding

BB/N005570/1
BB/R013993/1

Author’s competing interest statement

No conflict of Interest.

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