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Structural and functional properties of designed globins |
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| Authors: | Yasuhiro Isogai Anna Ishii Manabu Ishida Masahiro Mukai Motonori Ota Ken Nishikawa and Tetsutaro Iizuka |
| Institution: | (1) RIKEN (The Institute of Physical and Chemical Research), 2-1 Hirosawa, 351-0198 Wako, Saitama, Japan;(2) Department of Physics, Gakushuin University, Mejiro, 170-0031 Toshima-ku, Tokyo, Japan;(3) Department of Materials Chemistry, Faculty of Engineering, Hosei University, 3-7-2 Kajino-cho, 184-8584 Koganei-shi, Tokyo, Japan;(4) National Institute of Genetics, Yata, 411-8540 Mishima, Shizuoka, Japan |
| Abstract: | De novo design of artificial proteins is an essential approach to elucidate the principles of protein architecture and to understand specific functions of natural proteins and also to yield novel molecules for medical and industrial aims. We have designed artificial sequences of 153 amino acids to fit the main-chain framework of the sperm whale myoglobin structure based on the knowledge-based energy functions to evaluate the compatibility between protein tertiary structures and amino acid sequences. The synthesized artificial globins bind a single heme per protein molecule as designed, which show well-defined electrochemical and spectroscopic features characteristic of proteins with a low-spin heme. Redox and ligand binding reactions of the artificial heme proteins were investigated and these heme-related functions were found to vary with their structural uniqueness. Relationships between the structural and functional properties are discussed. |
| Keywords: | Heme myoglobin protein design structure and function |
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