Histidine side-chain dynamics and protonation monitored by C-13 CPMG NMR relaxation dispersion

Research output: Contribution to journalJournal article – Annual report year: 2009Researchpeer-review

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The use of C-13 NMR relaxation dispersion experiments to monitor micro-millisecond fluctuations in the protonation states of histidine residues in proteins is investigated. To illustrate the approach, measurements on three specifically C-13 labeled histidine residues in plastocyanin (PCu) from Anabaena variabilis (A.v.) are presented. Significant Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion is observed for C-13(epsilon 1) nuclei in the histidine imidazole rings of A.v. PCu. The chemical shift changes obtained from the CPMG dispersion data are in good agreement with those obtained from the chemical shift titration experiments, and the CPMG derived exchange rates agree with those obtained previously from N-15 backbone relaxation measurements. Compared to measurements of backbone nuclei, C-13(epsilon 1) dispersion provides a more direct method to monitor interchanging protonation states or other kinds of conformational changes of histidine side chains or their environment. Advantages and shortcomings of using the C-13(epsilon 1) dispersion experiments in combination with chemical shift titration experiments to obtain information on exchange dynamics of the histidine side chains are discussed.
Original languageEnglish
JournalJournal of Biomolecular N M R
Volume44
Issue number4
Pages (from-to)225-233
ISSN0925-2738
DOIs
Publication statusPublished - 2009
CitationsWeb of Science® Times Cited: No match on DOI

    Research areas

  • Plastocyanin, C-13 CPMG NMR relaxation dispersion, Histidine side-chain dynamics
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