Issue 16, 2017

NMR studies of the interactions between AMB-1 Mms6 protein and magnetosome Fe3O4 nanoparticles

Abstract

Mms6 protein from magnetotactic bacteria strain AMB-1 is responsible for controlling the formation of magnetite nanoparticles both in vitro and in vivo. High-resolution NMR studies showed the C-terminal DEEVE motif and the following residues undergoing conformation change upon magnetosome Fe3O4 crystal binding. The N-terminal hydrophobic packing of Mms6 protein is important for arranging the DEEVE motifs into a correct assembly and orientation that are crucial for magnetite crystal recognition.

Graphical abstract: NMR studies of the interactions between AMB-1 Mms6 protein and magnetosome Fe3O4 nanoparticles

Supplementary files

Article information

Article type
Paper
Submitted
28 Feb 2017
Accepted
17 Mrz 2017
First published
22 Mrz 2017

J. Mater. Chem. B, 2017,5, 2888-2895

NMR studies of the interactions between AMB-1 Mms6 protein and magnetosome Fe3O4 nanoparticles

K. Ma, H. Zhao, X. Zheng, H. Sun, L. Hu, L. Zhu, Y. Shen, T. Luo, H. Dai and J. Wang, J. Mater. Chem. B, 2017, 5, 2888 DOI: 10.1039/C7TB00570A

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements