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Conformational changes at the tetramerization site of erythroid α-spectrin upon binding β-spectrin: a spin label EPR study
We used cysteine scanning, isothermal titration calorimetry (ITC) and spin label EPR methods to study the two regions that flank the partial domain Helix C′ of the N-terminal end of α-spectrin (residues 14 – 20 and residues 44 – 54) in the absence and presence of a model protein of the β-spectrin C-...
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| 主要な著者: | , , |
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| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
2008
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2659877/ https://ncbi.nlm.nih.gov/pubmed/18783249 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi800840p |
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