Abstract
The effect of a nonsteroidal anti-inflammatory drug, the indomethacin, on the conformation of human serum albumin is investigated by evaluatingα-helix,β-structure and random coil structure contents from optical rotatory dispersion spectra. The observed structural changes may be attributed to theα-helix-to-β-structure conversion, because the content of random coil is not largely changed. The increase inβ-structure is due to a loss in the degrees of freedom in albumin.
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Cots, J., Pouplana, R. & Estelrich, J. Conformational changes in the human serum albumin-indomethacin binding. Colloid & Polymer Sci 265, 164–166 (1987). https://doi.org/10.1007/BF01412760
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DOI: https://doi.org/10.1007/BF01412760