CID fragmentation, H/D exchange and supermetallization of Barnase-Barstar complex

Abstract The barnase-barstar complex is one of the most stable protein-protein complexes and has a very wide range of possible applications. Here we report the use of top-down mass spectrometry for the investigation of the structure of this complex, its ionization via ESI, isolation and fragmentatio...

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Autores principales:	Yury Kostyukevich, Aleksej A. Shulga, Alexey Kononikhin, Igor Popov, Eugene Nikolaev, Sergey Deyev
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/77f8348d5f064225bbb7d7bad1a76ed0
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spelling	oai:doaj.org-article:77f8348d5f064225bbb7d7bad1a76ed02021-12-02T16:06:46ZCID fragmentation, H/D exchange and supermetallization of Barnase-Barstar complex10.1038/s41598-017-06507-22045-2322https://doaj.org/article/77f8348d5f064225bbb7d7bad1a76ed02017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-06507-2https://doaj.org/toc/2045-2322Abstract The barnase-barstar complex is one of the most stable protein-protein complexes and has a very wide range of possible applications. Here we report the use of top-down mass spectrometry for the investigation of the structure of this complex, its ionization via ESI, isolation and fragmentation. It was found that the asymmetry of the resulting charge state distributions of the protein monomer product ions increased as the charge state of the precursor ions increased. For the investigation of the 3D structure of the complex, the gas phase H/D exchange reaction was used. In addition, supermetallized ions of the complex with Zn were produced and investigated. It was observed that an increase in the number of metals bound to the complex results in a change in complex stability and the charge distribution between protein fragment. Analysis of the fragmentation pattern of the supermetallized complex [bn-b* + 5Zn]10+ indicated that this ion is present in different conformations with different charges and Zn distributions. Since Zn cannot migrate, such structures must be formed during ionization.Yury KostyukevichAleksej A. ShulgaAlexey KononikhinIgor PopovEugene NikolaevSergey DeyevNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-9 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Yury Kostyukevich Aleksej A. Shulga Alexey Kononikhin Igor Popov Eugene Nikolaev Sergey Deyev CID fragmentation, H/D exchange and supermetallization of Barnase-Barstar complex
description	Abstract The barnase-barstar complex is one of the most stable protein-protein complexes and has a very wide range of possible applications. Here we report the use of top-down mass spectrometry for the investigation of the structure of this complex, its ionization via ESI, isolation and fragmentation. It was found that the asymmetry of the resulting charge state distributions of the protein monomer product ions increased as the charge state of the precursor ions increased. For the investigation of the 3D structure of the complex, the gas phase H/D exchange reaction was used. In addition, supermetallized ions of the complex with Zn were produced and investigated. It was observed that an increase in the number of metals bound to the complex results in a change in complex stability and the charge distribution between protein fragment. Analysis of the fragmentation pattern of the supermetallized complex [bn-b* + 5Zn]10+ indicated that this ion is present in different conformations with different charges and Zn distributions. Since Zn cannot migrate, such structures must be formed during ionization.
format	article
author	Yury Kostyukevich Aleksej A. Shulga Alexey Kononikhin Igor Popov Eugene Nikolaev Sergey Deyev
author_facet	Yury Kostyukevich Aleksej A. Shulga Alexey Kononikhin Igor Popov Eugene Nikolaev Sergey Deyev
author_sort	Yury Kostyukevich
title	CID fragmentation, H/D exchange and supermetallization of Barnase-Barstar complex
title_short	CID fragmentation, H/D exchange and supermetallization of Barnase-Barstar complex
title_full	CID fragmentation, H/D exchange and supermetallization of Barnase-Barstar complex
title_fullStr	CID fragmentation, H/D exchange and supermetallization of Barnase-Barstar complex
title_full_unstemmed	CID fragmentation, H/D exchange and supermetallization of Barnase-Barstar complex
title_sort	cid fragmentation, h/d exchange and supermetallization of barnase-barstar complex
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/77f8348d5f064225bbb7d7bad1a76ed0
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CID fragmentation, H/D exchange and supermetallization of Barnase-Barstar complex

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