総説
光解離に伴うヘモグロビンの動きを観る
2004 年 44 巻 3 号 p. 108-112
詳細
2004 年 44 巻 3 号 p. 108-112
The binding of ligands by proteins is accompanied by rapid structural changes that are essential to function. A recent crystallographic study has revealed the ligation-linked protein motions in an allosteric protein, human hemoglobin, in both allosteric forms (T and R) upon photolysis of bound CO at cryogenic temperatures. The results show how differently the α and β subunits, within each allosteric form, respond to loss of ligand, and where the free ligand lies, establishing that the mechanism of protein control of ligand binding is radically different between the subunits.
