Mass spectrometry beyond the native state.

Autor: Chandler SA; Department of Chemistry, Physical & Theoretical Chemistry Laboratory, University of Oxford, Oxford OX1 3QZ, UK., Benesch JL; Department of Chemistry, Physical & Theoretical Chemistry Laboratory, University of Oxford, Oxford OX1 3QZ, UK. Electronic address: justin.benesch@chem.ox.ac.uk.
Jazyk: angličtina
Zdroj: Current opinion in chemical biology [Curr Opin Chem Biol] 2018 Feb; Vol. 42, pp. 130-137. Date of Electronic Publication: 2017 Dec 27.
DOI: 10.1016/j.cbpa.2017.11.019
Abstrakt: Native mass spectrometry allows the study of proteins by probing in vacuum the interactions they form in solution. It is a uniquely useful approach for structural biology and biophysics due to the high resolution of separation it affords, allowing the concomitant interrogation of multiple protein components with high mass accuracy. At its most basic, native mass spectrometry reports the mass of intact proteins and the assemblies they form in solution. However, the opportunities for more detailed characterisation are extensive, enabled by the exquisite control of ion motion that is possible in vacuum. Here we describe recent developments in mass spectrometry approaches to the structural interrogation of proteins both in, and beyond, their native state.
(Copyright © 2017 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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