The electronic structure of human erythropoietin as an aid in the design of oxidation-resistant therapeutic proteins

研究成果: Article査読

4 被引用数 (Scopus)

抄録

The electronic structure of human erythropoietin (HuEPO) has been investigated with the aid of quantum mechanical calculations. The results indicate that the protein is highly polarized and its permanent dipole moment has a magnitude of 471 D. The HOMO of HuEPO is localized on Trp51, which stays in close proximity to Met54. Three oxidation-resistant mutants of HuEPO (W51F, M54V, and W51F-M54V) have been modeled and their electronic structures are compared to that of the native protein. Among them, the W51F mutation is predicted to be the most effective in increasing the oxidation potential of the protein.

本文言語English
ページ(範囲)587-591
ページ数5
ジャーナルBioorganic and Medicinal Chemistry Letters
16
3
DOI
出版ステータスPublished - 2006 2月 1

ASJC Scopus subject areas

  • 生化学
  • 分子医療
  • 分子生物学
  • 薬科学
  • 創薬
  • 臨床生化学
  • 有機化学

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