Structural and dynamic studies of two antigenic loops from haemagglutinin: a relaxation matrix approach.

摘要: We have investigated the dynamics and structural behaviour of two antigenic peptides using 1H NMR. The cyclic mimic site A influenza haemagglutinin protein; they only differ in way were cyclized size their respective linkers. Homonuclear relaxation parameters extracted from a complete NOE matrix interpreted terms local dynamics. set distance constraints was deduced these which allowed 3D models to be constructed geometry. back-calculation used check validity final models. Strong variations internal motion amplitude been found both along backbone. Motions with high amplitudes localized Gly-Pro-Gly sequence forms β-turn structures.