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Sci Rep. 2017 Jul 21;7(1):6176. doi: 10.1038/s41598-017-06507-2.

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

Author information

1
Skolkovo Institute of Science and Technology Novaya St., 100, Skolkovo, 143025, Russian Federation.
2
Institute for Energy Problems of Chemical Physics, Russian Academy of Sciences, Leninskij pr. 38, k.2, 119334, Moscow, Russia.
3
Emanuel Institute for Biochemical Physics, Russian Academy of Sciences Kosygina st. 4, 119334, Moscow, Russia.
4
Moscow Institute of Physics and Technology, 141700, Dolgoprudnyi, Moscow Region, Russia.
5
Shemyakin & Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, 16/10, Miklukho-Maklaya str., Moscow, 117997, Russian Federation.
6
Skolkovo Institute of Science and Technology Novaya St., 100, Skolkovo, 143025, Russian Federation. ennikolaev@rambler.ru.
7
Institute for Energy Problems of Chemical Physics, Russian Academy of Sciences, Leninskij pr. 38, k.2, 119334, Moscow, Russia. ennikolaev@rambler.ru.
8
Emanuel Institute for Biochemical Physics, Russian Academy of Sciences Kosygina st. 4, 119334, Moscow, Russia. ennikolaev@rambler.ru.
9
Moscow Institute of Physics and Technology, 141700, Dolgoprudnyi, Moscow Region, Russia. ennikolaev@rambler.ru.
10
National Research Tomsk Polytechnic University, 30, av. Lenina, Tomsk, 634050, Russia.

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.

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