Molecular Dynamics-Derived Coloured Noise Mediates Anderson Localisation and Environment-Assisted Transport of Tryptophan Excitons in Tubulin

The tryptophan residues in tubulin αβ-dimers form an ordered aromatic network that has been proposed to support quantum exciton transport even under physiological environmental noise. Existing studies of this system mostly assume white-noise dephasing, but the statistical properties of the protein-solvent bath coupled to tryptophan sites remain uncharacterised under physiological conditions. Here we characterise this fluctuation bath via all-atom molecular dynamics simulations of a solvated tubulin dimer at 310 K, combining high-frequency and long-time trajectories with 10 fs and 10 ps sampling intervals. The resulting autocorrelation of the site-energy fluctuations is tri-exponential, with three well-separated decay modes: sub-100-fs and picosecond fluctuations driven by water dynamics, and a nanosecond mode originating from protein conformational rearrangements. All three modes fall deep within the non-Markovian regime. We further demonstrate that the slow protein mode introduces strong quasi-static disorder, which results in Anderson localisation, while the two fast water modes frequently tune chromophore pairs through resonance, enabling environment-assisted quantum transport (ENAQT). On the full eight-site network, the coloured-noise bath confines excitons predominantly to strongly coupled proximal tryptophan pairs, in marked contrast to the more uniform delocalisation predicted by the standard white-noise Haken-Strobl model. Our workflow generalises to other pigment-protein systems with solvent-exposed chromophores.