Ion mobility mass spectrometry and molecular dynamics simulations unravel the conformational stability of zinc metallothionein-2 species-Reference-Cited by-同舟云学术

Ion mobility mass spectrometry and molecular dynamics simulations unravel the conformational stability of zinc metallothionein-2 species

Published:2023 Issue:30 Volume:59 Page:4471-4474
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Peris-Díaz Manuel David¹²^ORCID,Barkhanskiy Alexey²,Liggett Ellen²,Barran Perdita²^ORCID,Krężel Artur¹^ORCID

Affiliation:

1. Department of Chemical Biology, Faculty of Biotechnology, University of Wrocław, F. Joliot-Curie 14a, 50-383 Wrocław, Poland

2. Michael Barber Centre for Collaborative Mass Spectrometry, Manchester Institute of Biotechnology, 131 Princess Street, Manchester, M1 7DN, UK

Abstract

We present a molecular dynamics approach to explore the conformational landscape of proteins analyzed by ion mobility-mass spectrometry, providing new insights into the structural properties of metallothioneins, a cellular zinc buffer system.

Funder

Narodowe Centrum Nauki

Engineering and Physical Sciences Research Council

European Research Council

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2023/CC/D2CC06559B

Reference27 articles.

1. The Functions of Metamorphic Metallothioneins in Zinc and Copper Metabolism

2. Metallothioneins

3. Metal binding and interdomain thermodynamics of mammalian metallothionein-3: enthalpically favoured Cu⁺ supplants entropically favoured Zn²⁺ to form Cu₄⁺ clusters under physiological conditions

4. The Bioinorganic Chemistry of Mammalian Metallothioneins

5. Mammalian MT1 and MT2 metallothioneins differ in their metal binding abilities

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