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Mechanism of protein folding: I. General considerations and refolding of myoglobin |
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| Authors: | Nobuhiko Sait Takao Shigaki Yutaka Kobayashi Masahiko Yamamoto |
| Institution: | Department of Applied Physics, Waseda University, Tokyo, Japan. |
| Abstract: | To explain the rapidity of the process of protein folding, we cite two aspects of hydrophobic interaction: its long-range nature and the specificity of pairing after the formation of secondary structures. These two factors, when incorporated with the growth-type mechanism, can determine the folding pathway of proteins. This mechanism is applied to myoglobin. Appropriate introduction of side chains of amino acid residues and the heme group attached to His 93 yield a refolded tertiary structure that is in good agreement with the native structure. |
| Keywords: | folding pathway hydrophobic interaction long-range and long-distance interactions secondary structure tertiary structure module structure |