Issue 30, 2017
From the journal:

Chemical Communications

The metalation of hen egg white lysozyme impacts protein stability as shown by ion mobility mass spectrometry, differential scanning calorimetry, and X-ray crystallography†

Matthew P. Sullivan, ORCID logo ab   Michael Groessl,c   Samuel M. Meier, ORCID logo d   Richard L. Kingston,b   David C. Goldstoneb  and  Christian G. Hartinger ORCID logo *a  

* Corresponding authors

a School of Chemical Sciences, University of Auckland, Private Bag 92019, Auckland, New Zealand
E-mail: c.hartinger@auckland.ac.nz
Web: http://www.hartinger.auckland.ac.nz/

b School of Biological Sciences, University of Auckland, Private Bag 92019, Auckland, New Zealand

c TOFWERK, Uttigenstr. 22, Thun, Switzerland

d Institute of Analytical Chemistry, University of Vienna, Waehringer Str. 38, Vienna, Austria

Abstract

Metalation of hen egg white lysozyme (HEWL) with organometallics was studied with physicochemical methods in solid state, solution and the gas phase. While metalation did not affect the crystal structure of HEWL significantly, protein destabilisation was detected in gas phase and solution.

Graphical abstract: The metalation of hen egg white lysozyme impacts protein stability as shown by ion mobility mass spectrometry, differential scanning calorimetry, and X-ray crystallography

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Article information

DOI
https://doi.org/10.1039/C6CC10150J
Article type
Communication
Submitted
22 Dec 2016
Accepted
16 Mar 2017
First published
21 Mar 2017

Chem. Commun., 2017,53, 4246-4249

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The metalation of hen egg white lysozyme impacts protein stability as shown by ion mobility mass spectrometry, differential scanning calorimetry, and X-ray crystallography

M. P. Sullivan, M. Groessl, S. M. Meier, R. L. Kingston, D. C. Goldstone and C. G. Hartinger, Chem. Commun., 2017, 53, 4246 DOI: 10.1039/C6CC10150J

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