Dongping Zhong

TL;DR: The direct mapping of global hydration dynamics around a protein in its native and molten globular states, using a tryptophan scan by site-specific mutations, reveals the intimate relationship betweenhydration dynamics and protein fluctuations and such biologically relevant water–protein interactions fluctuate on picosecond time scales.

TL;DR: In this article, the authors provide a critique of the hydration dynamics of macromolecules, particularly those of protein and DNA, and maintain that there are two types of water hydration, those that reorient in the vicinity of the surface and those which are ordered.

TL;DR: Experimental and theoretical studies on water and protein dynamics following photoexcitation of apomyoglobin revealed the molecular mechanism of slow hydration processes and elucidated the role of protein fluctuations.

TL;DR: In this article, a femtosecond synchronization of the enzymatic dynamics with the repair function is reported, which shows that the photocycle of DNA repair by photolyase is through a radical mechanism and completed on subnanosecond time scale at the dynamic active site, with no net change in the redox state of the flavin cofactor.

TL;DR: These observed distinct dynamics, controlled by the flavin ring flexibility, are fundamental to flavoenzyme's functions, as observed in photolyase with a planar structure to lengthen the lifetime to maximize DNA repair efficiency and in insect type 1 cryptochrome with a flexible structure to vary the excited-state deactivation to modulate the functional channel.