@article{oai:repo.qst.go.jp:00043927,
 author = {Kurihara, Yasuyuki and Katahira, Masato and Saito, Toshiyuki and Uesugi, Seiichi and et.al and 齋藤 俊行},
 journal = {Journal of Biochemistry},
 month = {Oct},
 note = {Max is a basic region/helix-loop-helix/leucine zipper (b/HLH/Z) protein that forms a hetero-complex with the Myc family proteins Myc, Mad, and Mxi1, and a homo-complex with itself. These complexes specifically bind to double-stranded DNA containing CACGTG sequences. Here, we report on the structural properties in aqueous solution of a 109-amino-acid protein, Max110, corresponding to the N-terminal domain of Max containing the b/HLH/Z motif (residues 2-110), as characterized by combined use of circular dichroism (CD) and sedimentation equilibrium experiments. The results showed that the alpha-helical content of Max110 increases with increasing protein concentration. The sedimentation equilibrium data indicated that Max110 exists as a monomer at low protein concentration, and forms a dimer at high protein concentration. Further increases in the alpha-helical content of Max110 occur upon addition of DNA with the CACGTG recognition sequence. Thus, dimerization and binding to DNA of Max both favor an increase of the alpha-helical content.},
 pages = {711--716},
 title = {Dimerization and DNA binding facilitate alpha-helix formation of Max in solution.},
 volume = {122},
 year = {1997}
}