TY - JOUR
T1 - Gradual crossover from subdiffusion to normal diffusion
T2 - a many-body effect in protein surface water
AU - Tan, Pan
AU - Liang, Yihao
AU - Xu, Qin
AU - Mamontov, Eugene
AU - Li, Jinglai
AU - Xing, Xiangjun
AU - Hong, Liang
PY - 2018/6/15
Y1 - 2018/6/15
N2 - Dynamics of hydration water is essential for the function of biomacromolecules. Previous studies have demonstrated that water molecules exhibit subdiffusion on the surface of biomacromolecules; yet the microscopic mechanism remains vague. Here, by performing neutron scattering, molecular dynamics simulations, and analytic modeling on hydrated perdeuterated protein powders, we found water molecules jump randomly between trapping sites on protein surfaces, whose waiting times obey a broad distribution, resulting in subdiffusion. Moreover, the subdiffusive exponent gradually increases with observation time towards normal diffusion due to a many-body volume-exclusion effect.
AB - Dynamics of hydration water is essential for the function of biomacromolecules. Previous studies have demonstrated that water molecules exhibit subdiffusion on the surface of biomacromolecules; yet the microscopic mechanism remains vague. Here, by performing neutron scattering, molecular dynamics simulations, and analytic modeling on hydrated perdeuterated protein powders, we found water molecules jump randomly between trapping sites on protein surfaces, whose waiting times obey a broad distribution, resulting in subdiffusion. Moreover, the subdiffusive exponent gradually increases with observation time towards normal diffusion due to a many-body volume-exclusion effect.
U2 - 10.1103/physrevlett.120.248101
DO - 10.1103/physrevlett.120.248101
M3 - Article
SN - 0031-9007
VL - 120
JO - Physical Review Letters
JF - Physical Review Letters
IS - 24
M1 - 248101
ER -