Reproduced with permission from  Hinge-Bending Motions of Dynamic Domains To investigate the relationship between the unfolding behavior and the struc- tural dynamics of goat α-lactalbumin, we carried out a principal component analysis of the MD trajectories for the equilibrium dynamics at 298K and unfolding dynamics at 398 K, and characterized the principal modes as screw motions of dynamic domains according to the method of Hayward et al.
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