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Mechanism of protein folding: I. General considerations and refolding of myoglobin
Author(s) -
Saitô Nobuhiko,
Shigaki Takao,
Kobayashi Yutaka,
Yamamoto Masahiko
Publication year - 1988
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340030308
Subject(s) - myoglobin , chemistry , folding (dsp implementation) , mechanism (biology) , protein folding , protein tertiary structure , heme , protein secondary structure , side chain , biophysics , stereochemistry , crystallography , biochemistry , organic chemistry , biology , physics , electrical engineering , enzyme , engineering , quantum mechanics , polymer
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 chins 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.