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 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.

journal_name

Sci Rep

journal_title

Scientific reports

authors

Kostyukevich Y,Shulga AA,Kononikhin A,Popov I,Nikolaev E,Deyev S

doi

10.1038/s41598-017-06507-2

subject

Has Abstract

pub_date

2017-07-21 00:00:00

pages

6176

issue

1

issn

2045-2322

pii

10.1038/s41598-017-06507-2

journal_volume

7

pub_type

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