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Report No.

Nanosecond structural dynamics of intrinsically disordered $$beta$$-casein micelles by neutron spectroscopy

Nakagawa, Hiroshi   ; Appavou, M.-S.*; Wuttke, J.*; Zamponi, M.*; Holderer, O.*; Schrader, T. E.*; Richter, D.*; Doster, W.*

Casein proteins are characterized by its extended structural features and its dynamics, which are different from those of typical folded proteins, due to a large number of proline residues. We were able to describe the unique structural dynamics by Orenstein-Uhlenbeck Brownian oscillator model by several types of QENS experiments with wide time-scales. The characterized dynamics also allowed us to discuss the effective sequestration of calcium phosphate in terms of its unique dynamical structure. The biological role of the physical processes of the proteins on the nanosecond order on the biological functions is presented.



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