Measuring inter-protein pairwise interaction energies from a single native mass spectrum by double-mutant cycle analysis

Miri Sokolovski, Jelena Cveticanin, Déborah Hayoun, Ilia Korobko, Michal Sharon () and Amnon Horovitz ()
Additional contact information
Miri Sokolovski: Weizmann Institute of Science
Jelena Cveticanin: Weizmann Institute of Science
Déborah Hayoun: Weizmann Institute of Science
Ilia Korobko: Weizmann Institute of Science
Michal Sharon: Weizmann Institute of Science
Amnon Horovitz: Weizmann Institute of Science

Nature Communications, 2017, vol. 8, issue 1, 1-7

Abstract: Abstract The strength and specificity of protein complex formation is crucial for most life processes and is determined by interactions between residues in the binding partners. Double-mutant cycle analysis provides a strategy for studying the energetic coupling between amino acids at the interfaces of such complexes. Here we show that these pairwise interaction energies can be determined from a single high-resolution native mass spectrum by measuring the intensities of the complexes formed by the two wild-type proteins, the complex of each wild-type protein with a mutant protein, and the complex of the two mutant proteins. This native mass spectrometry approach, which obviates the need for error-prone measurements of binding constants, can provide information regarding multiple interactions in a single spectrum much like nuclear Overhauser effects (NOEs) in nuclear magnetic resonance. Importantly, our results show that specific inter-protein contacts in solution are maintained in the gas phase.

Date: 2017
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-017-00285-1 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-00285-1

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-017-00285-1

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().