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In the early 1940s, five students and a professor secretly wrote and distributed pamphlets calling on Germans to resist Hitler. This book presents facsimiles and transcriptions of the original pamphlets alongside a new collaborative translation by students. A series of essays by experts on the White Rose examines the group members’ lives and legacy.

In the early 1940s, five students and a professor secretly wrote and distributed pamphlets calling on Germans to resist Hitler. This book presents facsimiles and transcriptions of the original pamphlets alongside a new collaborative translation by students. A series of essays by experts on the White Rose examines the group members’ lives and legacy.

We examine temperature dependent picosecond dynamics as a function of structure and function for lysozyme and cytochrome c using temperature dependent terahertz permittivity measurements. A double Arrhenius temperature dependence with activation energies E1 ~ 0.1 kJ/mol and E2 ~10 kJ/mol fits the native state response. The higher activation energy is consistent with the so-called protein dynamical transition associated with beta relaxations at the solvent-protein interface. The lower activation energy is consistent with correlated structural motions. When the structure is removed by denaturing the lower activation energy process is no longer present. Additionally the lower activation energy process is diminished with ligand binding, but not for changes in internal oxidation state. We suggest that the lower energy activation process is associated with collective structural motions that are no longer accessible with denaturing or binding., Comment: 4 main pages, 3 figures, 1 table, 2 supplemental tables