Hydrophobic scale: a second parameter to elucidating various specific ligand-protein interactions.
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.
Numao
Naganori
N
BioFrontier Institute Inc, Kanagawa, Japan. numao-n@sssc.co.jp
Fujii
Hisashi
H
Fukazawa
Yoshiyuki
Y
Hanagata
Nobutaka
N
Tanaka
Kazuyoshi
K
D000595:Amino Acid Sequence; D000818:Animals; D019485:Bone Morphogenetic Proteins / Q000737:chemistry; D004330:Drosophila / Q000737:chemistry; D004926:Escherichia coli / Q000737:chemistry; D005346:Fibroblast Growth Factors / Q000737:chemistry; D005583:Fourier Analysis; D006801:Humans; D008024:Ligands; D051379:Mice; D008958:Models, Molecular; D009711:Nucleotides / Q000737:chemistry; D012275:Oryza / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D012441:Saccharomyces cerevisiae / Q000737:chemistry; D017421:Sequence Analysis; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry
D019485:Bone Morphogenetic Proteins; D008024:Ligands; D009711:Nucleotides; D011506:Proteins; D016159:Tumor Suppressor Protein p53; D005346:Fibroblast Growth Factors