The influence of protein dynamics on Mössbauer spectra

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Abstract
Proteindynamics gives rise to characteristic changes in a Mössbauer spectrum. The spectra are analyzed by a minimum of three Brownian oscillator modes accounting for protein specific motion probed by the Mössbauer nucleus. Two of these modes are extremely overdamped; a third mode has a diffusionlike character. The drastic changes of the Mössbauer spectrum with temperature are simulated by an extended version of the Brownian oscillator. With this oscillator the protein is characterized by conformational substates and transition states. The first are responsible for the solidlike, the latter for the liquidlike behavior of the protein. The interplay of transition states and conformational substates is responsible for largely different temperature dependences of the mean square displacements from x‐ray and Mössbauer experiments.