Nanosecond structural dynamics of intrinsically disordered β-casein micelles by neutron spectroscopy.

ABSTRACT: β-casein undergoes a reversible endothermic self-association, forming protein micelles of limited size. In its functional state, a single β-casein monomer is unfolded, which creates a high structural flexibility, which is supposed to play a major role in preventing the precipitation of calcium phosphate particles. We characterize the structural flexibility in terms of nanosecond molecular motions, depending on the temperature by quasielastic neutron scattering. Our major questions are: Does the self-association reduce the chain flexibility? How does the dynamic spectrum of disordered caseins differ from a compactly globular protein? How does the dynamic spectrum of β-casein in solution differ from that of a protein in hydrated powder states? We report on two relaxation processes on a nanos

SUBMITTER: Nakagawa H 

PROVIDER: S-EPMC8715185 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature