Hydrophobic scale: a second parameter to elucidating various specific ligand-protein interactions |
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Authors: | Numao Naganori Fujii Hisashi Fukazawa Yoshiyuki Hanagata Nobutaka Tanaka Kazuyoshi |
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Institution: | BioFrontier Institute Inc, Kanagawa, Japan. numao-n@sssc.co.jp |
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Abstract: | In the sequence Fourier analysis (SFA) of specific interactions such as those between fibroblast growth factors (FGFs)/FGF receptors (FGFRs), bone morphogenetic proteins (BMPs)/BMP receptors (BMPRs), or tumor repressor protein p53/mouse double minute 2 homolog (MDM2), the characteristic frequency peak(s) could be observed with the hydrophobic scale for 20 amino acids as well as 4 nucleotides as the physicochemical parameter, but not successfully with the absolute electronegativity scale. This result implies that these two independent scales should be appropriately selected in various specific ligand-protein interactions, though the critical difference has to be determined. |
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