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

Double mutant cycle (DMC) analyses can provide the interaction energies between amino acids at the interface of protein complexes. Here, the authors determine pairwise interaction energies using high-resolution native mass spectroscopy, offering a straightforward route for the DMC methodology.

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Autores principales: Miri Sokolovski, Jelena Cveticanin, Déborah Hayoun, Ilia Korobko, Michal Sharon, Amnon Horovitz
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2017
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Acceso en línea:https://doaj.org/article/4a25bcb5b7644dde90dc2233ecee1ba5
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spelling oai:doaj.org-article:4a25bcb5b7644dde90dc2233ecee1ba52021-12-02T10:48:28ZMeasuring inter-protein pairwise interaction energies from a single native mass spectrum by double-mutant cycle analysis10.1038/s41467-017-00285-12041-1723https://doaj.org/article/4a25bcb5b7644dde90dc2233ecee1ba52017-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-00285-1https://doaj.org/toc/2041-1723Double mutant cycle (DMC) analyses can provide the interaction energies between amino acids at the interface of protein complexes. Here, the authors determine pairwise interaction energies using high-resolution native mass spectroscopy, offering a straightforward route for the DMC methodology.Miri SokolovskiJelena CveticaninDéborah HayounIlia KorobkoMichal SharonAmnon HorovitzNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-7 (2017)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Miri Sokolovski
Jelena Cveticanin
Déborah Hayoun
Ilia Korobko
Michal Sharon
Amnon Horovitz
Measuring inter-protein pairwise interaction energies from a single native mass spectrum by double-mutant cycle analysis
description Double mutant cycle (DMC) analyses can provide the interaction energies between amino acids at the interface of protein complexes. Here, the authors determine pairwise interaction energies using high-resolution native mass spectroscopy, offering a straightforward route for the DMC methodology.
format article
author Miri Sokolovski
Jelena Cveticanin
Déborah Hayoun
Ilia Korobko
Michal Sharon
Amnon Horovitz
author_facet Miri Sokolovski
Jelena Cveticanin
Déborah Hayoun
Ilia Korobko
Michal Sharon
Amnon Horovitz
author_sort Miri Sokolovski
title Measuring inter-protein pairwise interaction energies from a single native mass spectrum by double-mutant cycle analysis
title_short Measuring inter-protein pairwise interaction energies from a single native mass spectrum by double-mutant cycle analysis
title_full Measuring inter-protein pairwise interaction energies from a single native mass spectrum by double-mutant cycle analysis
title_fullStr Measuring inter-protein pairwise interaction energies from a single native mass spectrum by double-mutant cycle analysis
title_full_unstemmed Measuring inter-protein pairwise interaction energies from a single native mass spectrum by double-mutant cycle analysis
title_sort measuring inter-protein pairwise interaction energies from a single native mass spectrum by double-mutant cycle analysis
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/4a25bcb5b7644dde90dc2233ecee1ba5
work_keys_str_mv AT mirisokolovski measuringinterproteinpairwiseinteractionenergiesfromasinglenativemassspectrumbydoublemutantcycleanalysis
AT jelenacveticanin measuringinterproteinpairwiseinteractionenergiesfromasinglenativemassspectrumbydoublemutantcycleanalysis
AT deborahhayoun measuringinterproteinpairwiseinteractionenergiesfromasinglenativemassspectrumbydoublemutantcycleanalysis
AT iliakorobko measuringinterproteinpairwiseinteractionenergiesfromasinglenativemassspectrumbydoublemutantcycleanalysis
AT michalsharon measuringinterproteinpairwiseinteractionenergiesfromasinglenativemassspectrumbydoublemutantcycleanalysis
AT amnonhorovitz measuringinterproteinpairwiseinteractionenergiesfromasinglenativemassspectrumbydoublemutantcycleanalysis
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