Self-assembly of toroidal proteins explored using native mass spectrometry-Reference-Cited by-同舟云学术

Self-assembly of toroidal proteins explored using native mass spectrometry

Published:2018 Issue:28 Volume:9 Page:6099-6106
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Yewdall N. Amy¹²³⁴⁵^ORCID,Allison Timothy M.⁶⁷⁸⁹,Pearce F. Grant¹²³⁴⁵,Robinson Carol V.⁶⁷⁸⁹^ORCID,Gerrard Juliet A.¹⁰¹¹¹¹²⁵^ORCID

Affiliation:

1. School of Biological Sciences

2. School of Chemical Sciences

3. University of Auckland

4. Auckland 1010

5. New Zealand

6. Department of Chemistry

7. University of Oxford

8. Oxford OX1 5QY

9. UK

10. Biomolecular Interaction Centre

11. University of Canterbury

12. Christchurch 8140

Abstract

The peroxiredoxins are a well characterised family of toroidal proteins which can self-assemble into a striking array of quaternary structures, including protein nanotubes, making them attractive as building blocks for nanotechnology.

Funder

Army Research Office

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2018/SC/C8SC01379A

Reference44 articles.

1. Toward complex matter: Supramolecular chemistry and self-organization

2. One ring (or two) to hold them all - on the structure and function of protein nanotubes

3. Bovine Mitochondrial Peroxiredoxin III Forms a Two-Ring Catenane

4. Structures of Human Peroxiredoxin 3 Suggest Self-Chaperoning Assembly that Maintains Catalytic State

5. The physics of protein self-assembly

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