Combined chemical modification and collision induced unfolding using native ion mobility‐mass spectrometry provides insights into protein gas‐phase structure

Al-jabiry, A., Palmer, M., Langridge, J., Bellamy-Carter, J., Robinson, D. ORCID: 0000-0003-2760-7163 and Oldham, N.J., 2021. Combined chemical modification and collision induced unfolding using native ion mobility‐mass spectrometry provides insights into protein gas‐phase structure. Chemistry – A European Journal. ISSN 0947-6539

[img] Text
1460468_Robinson.pdf - Post-print
Full-text access embargoed until 21 July 2022.

Download (1MB)

Abstract

Native mass spectrometry is now an important tool in structural biology. Thus, the nature of higher protein structure in the vacuum of the mass spectrometer is an area of significant interest. One of the major goals in the study of gas-phase protein structure is to elucidate the stabilising role of interactions at the level of individual amino acid residues. A strategy combining protein chemical modification together with collision induced unfolding (CIU) was developed and employed to probe the structure of compact protein ions produced by native electrospray ionisation. Tractable chemical modification was used to alter the properties of amino acid residues, and ion mobility-mass spectrometry (IM-MS) utilised to monitor the extent of unfolding as a function of modification. From these data the importance of specific intramolecular interactions for the stability of compact gas-phase protein structure can be inferred. Using this approach, and aided by molecular dynamics simulations, an important stabilising interaction between K6 and H68 in the protein ubiquitin was identified, as was a contact between the N-terminus and E22 in a ubiquitin binding protein UBA2.

Item Type: Journal article
Description: Received: 2021-05-26; Accepted: 2021-07-21; Published: 2021-07-21
Publication Title: Chemistry – A European Journal
Creators: Al-jabiry, A., Palmer, M., Langridge, J., Bellamy-Carter, J., Robinson, D. and Oldham, N.J.
Publisher: Wiley
Date: 21 July 2021
ISSN: 0947-6539
Identifiers:
NumberType
10.1002/chem.202101857DOI
1460468Other
Divisions: Schools > School of Science and Technology
Record created by: Jeremy Silvester
Date Added: 19 Aug 2021 08:58
Last Modified: 19 Aug 2021 08:58
URI: http://irep.ntu.ac.uk/id/eprint/44062

Actions (login required)

Edit View Edit View

Views

Views per month over past year

Downloads

Downloads per month over past year