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Solution NMR structures of oxidized and reduced Ehrlichia chaffeensis thioredoxin: NMR-invisible structure owing to backbone dynamics
Thioredoxins are small ubiquitous proteins that participate in a diverse variety of redox reactions via the reversible oxidation of two cysteine thiol groups in a structurally conserved active site. Here, the NMR solution structures of a reduced and oxidized thioredoxin from Ehrlichia chaffeensis (E...
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| Vydáno v: | Acta Crystallogr F Struct Biol Commun |
|---|---|
| Hlavní autoři: | , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
International Union of Crystallography
2018
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5947692/ https://ncbi.nlm.nih.gov/pubmed/29372907 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S2053230X1701799X |
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