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Article

Probing the influence of mutations on the stability of a ferredoxin by mass spectrometry.

Journal of protein chemistry - 1 Jul 1997

Rémigy H, Jaquinod M, Pétillot Y, Gagnon J, Cheng H, Xia B, Markley J L, Hurley J K, Tollin G, Forest E

Abstract excerpt

Hydrogen/deuterium exchange, which depends on solvent accessibility, can be probed by mass spectrometry (MS) to get information on protein conformation or protein-ligand interaction. In this work, the conformational properties of the cyanobacterium Anabaena wild-type ferredoxin as well as of two single-site mutants (Phe 65 Ala and Arg 42 Ala) were studied. After incubation of the wild type and mutant proteins in...

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Identifiers

PMID: 9246639
DOI: 10.1023/a:1026325914372

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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