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

研究成果: ジャーナルへの寄稿学術論文査読

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.

本文言語英語
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
出版ステータス出版済み - 2006 2月 1

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