Different segmental flexibility of human serum transferrin and lactoferrin

摘要: X-ray diffraction studies show that the diferric (holo) forms of human serum transferrin and lactoferrin have almost same conformation in crystal. In solution, however, two proteins exhibit different characteristics. The differences are even more pronounced apo forms. Small-angle neutron scattering data is less compact, holo forms, than corresponding solution. comparison primary structures suggests one interdomain hinge regions significantly longer its counterpart transferrin. difference flexibility due to long region may be responsible for many physicochemical characteristics proteins.