Origins of Apparent Fragile-to-Strong Transitions of Protein Hydration Waters

M. Vogel
Phys. Rev. Lett. 101, 225701 – Published 26 November 2008

Abstract

H2 NMR is used to study the mechanisms for the reorientation of protein hydration water. In the past, crossovers in temperature-dependent correlation times were reported at Tx1225K (X1) and Tx2200K (X2). We show that neither X1 nor X2 are related to a fragile-to-strong transition. Our results rule out an existence of X1. Also, they indicate that water performs thermally activated and distorted tetrahedral jumps at T<Tx2, implying that X2 originates in an onset of this motion, which may be related to a universal defect diffusion in materials with defined hydrogen-bond networks.

  • Figure
  • Figure
  • Figure
  • Received 10 June 2008

DOI:https://doi.org/10.1103/PhysRevLett.101.225701

©2008 American Physical Society

Authors & Affiliations

M. Vogel

  • Institut für Festkörperphysik, Technische Universität Darmstadt, Hochschulstr. 6, 64289 Darmstadt, Germany

Article Text (Subscription Required)

Click to Expand

References (Subscription Required)

Click to Expand
Issue

Vol. 101, Iss. 22 — 28 November 2008

Reuse & Permissions
Access Options
Author publication services for translation and copyediting assistance advertisement

Authorization Required


×
×

Images

×

Sign up to receive regular email alerts from Physical Review Letters

Log In

Cancel
×

Search


Article Lookup

Paste a citation or DOI

Enter a citation
×