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- W2019920544 abstract "Human macrophage migration inhibitory factor is a 114 amino acid protein that belongs to the family of immunologic cytokines. Assignments of 1H, l5N, and 13C resonances have enabled the determination of the secondary structure of the protein, which consists of two α-helices (residues 18–31 and 89–72) and a central four-stranded β-sheet. In the β -sheet, two parallel β -sheets are connected in an antiparallel sense. From the total of three cysteines present in the primary structure of MIF, none was found to form disulfide bridges. 1H-15N heteronuclear T1, T2, and steady-state NOE measurements indicate that the backbone of MIF exists in a rigid structure of limited conformational flexibility (on the nanosecond to picosecond time scale). Several residues located in the loop regions and at the N termini of two helices exhibit internal motions on the 1–3 ns time scale. The capacity to bind glutathione was investigated by titration of a uniform l5N-labeled sample and led us to conclude that MIF has, at best, very low affinity for glutathione." @default.
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- W2019920544 date "1996-10-01" @default.
- W2019920544 modified "2023-09-25" @default.
- W2019920544 title "NMR characterization of structure, backbone dynamics, and glutathione binding of the human macrophage migration inhibitory factor (MIF)" @default.
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- W2019920544 doi "https://doi.org/10.1002/pro.5560051016" @default.
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