Origins of Apparent Fragile-to-Strong Transitions of Protein Hydration Waters
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- 26 November 2008
- journal article
- research article
- Published by American Physical Society (APS) in Physical Review Letters
- Vol. 101 (22) , 225701
Abstract
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 () and (). We show that neither nor are related to a fragile-to-strong transition. Our results rule out an existence of . Also, they indicate that water performs thermally activated and distorted tetrahedral jumps at , implying that originates in an onset of this motion, which may be related to a universal defect diffusion in materials with defined hydrogen-bond networks.
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This publication has 30 references indexed in Scilit:
- Insights into Phases of Liquid Water from Study of Its Unusual Glass-Forming PropertiesScience, 2008
- Glass Transition in Biomolecules and the Liquid-Liquid Critical Point of WaterPhysical Review Letters, 2006
- Relaxation Processes in Supercooled Confined Water and Implications for Protein DynamicsPhysical Review Letters, 2006
- Observation of fragile-to-strong dynamic crossover in protein hydration waterProceedings of the National Academy of Sciences, 2006
- Pressure Dependence of Fragile-to-Strong Transition and a Possible Second Critical Point in Supercooled Confined WaterPhysical Review Letters, 2005
- Experimental evidence of a liquid-liquid transition in interfacial waterEurophysics Letters, 2005
- Dynamics of supercooled water in confined geometryNature, 2000
- Thermodynamic determination of fragility in liquids and a fragile-to-strong liquid transition in waterNature, 1999
- The relationship between liquid, supercooled and glassy waterNature, 1998
- Formation of Glasses from Liquids and BiopolymersScience, 1995