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  • Title: A circularly permuted myoglobin possesses a folded structure and ligand binding similar to those of the wild-type protein but with a reduced thermodynamic stability.
    Author: Fishburn AL, Keeffe JR, Lissounov AV, Peyton DH, Anthony-Cahill SJ.
    Journal: Biochemistry; 2002 Nov 05; 41(44):13318-27. PubMed ID: 12403634.
    Abstract:
    A circular permutein of sperm whale myoglobin in which the G helix is C-terminal, the H helix is N-terminal, and 16 amino acids link the H helix to the A helix has been expressed in Escherichia coli. The permutein sequence begins with Gly121 (using the numbering scheme for the wild-type protein) and terminates with Pro120. The ligand binding function of the permutein was assayed using stopped-flow methods and shown to be essentially identical to that of the wild-type protein. In addition, one- and two-dimensional NMR studies of the cyanomet isoform of the permutein show a nativelike structure with a heme binding pocket very similar to that of the wild-type myoglobin. Although the structure and function of the permutein resemble those of the wild-type myoglobin, the permutein is less stable to chemical denaturation by 5.2 kcal/mol.
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