Observation of fragile-to-strong dynamic crossover in protein hydration water.
At low temperatures, proteins exist in a glassy state, a state that has no conformational flexibility and shows no biological functions. In a hydrated protein, at temperatures greater-- similar 220 K, this flexibility is restored, and the protein is able to sample more conformational substates, thus becoming biologically functional. This "dynamical" transition of protein is believed to be triggered by its strong coupling with the hydration water, which also shows a similar dynamic transition. Here we demonstrate experimentally that this sudden switch in dynamic behavior of the hydration water on lysozyme occurs precisely at 220 K and can be described as a fragile-to-strong dynamic crossover. At the fragile-to-strong dynamic crossover, the structure of hydration water makes a transition from predominantly high-density (more fluid state) to low-density (less fluid state) forms derived from the existence of the second critical point at an elevated pressure.
Chen
S-H
SH
Department of Nuclear Science and Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. sowhsin@mit.edu
Liu
L
L
Fratini
E
E
Baglioni
P
P
Faraone
A
A
Mamontov
E
E
D000818:Animals; D002645:Chickens; D009113:Muramidase / Q000737:chemistry*; D009502:Neutrons; D011487:Protein Conformation; D013057:Spectrum Analysis / Q000379:methods; D013696:Temperature; D014867:Water / Q000737:chemistry*
D014867:Water; D009113:Muramidase