Observation of Fragile-to-Strong Dynamic Crossover in Protein Hydration Water

Details Observation of Fragile-to-Strong Dynamic Crossover in Protein Hydration Water Observation of Fragile-to-Strong Dynamic Crossover in Protein Hydration Water

2006-05-11

arxiv.org/abs/cond-mat/0605311v1

Physics

Condensed Matter

Soft Condensed Matter

6 pages (Latex), 4 figures (Postscript)

Scientific paper

10.1073/pnas.0602474103

At low temperatures proteins exist in a glassy state, a state which has no conformational flexibility and shows no biological functions. In a hydrated protein, at and above 220 K, this flexibility is restored and the protein is able to sample more conformational sub-states, thus becomes 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 (FSC). At FSC, the structure of hydration water makes a transition from predominantly high-density (more fluid state) to low-density (less fluid state) forms derived from existence of the second critical point at an elevated pressure.

Affiliated with

Also associated with

No associations

Rating

Observation of Fragile-to-Strong Dynamic Crossover in Protein Hydration Water does not yet have a rating. At this time, there are no reviews or comments for this scientific paper.

If you have personal experience with Observation of Fragile-to-Strong Dynamic Crossover in Protein Hydration Water, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Observation of Fragile-to-Strong Dynamic Crossover in Protein Hydration Water will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFWR-SCP-O-469427