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J. K. Kaushik and R. Bhat, “Why Is Trehalose an Exceptional Protein Stabilizer? An Analysis of the Thermal Stability of Proteins in the Presence of the Compatible Osmolyte Trehalose,” Journal of Biological Chemistry, Vol. 278, No. 29, 2003, pp. 26458-26465.doi:10.1074/jbc.M300815200

has been cited by the following article:

• TITLE: Dynamic and Configurational Approach to the Glass Transition by Nanoscale Cooperativity

  AUTHORS: G. Romeo

  KEYWORDS: Glass-Forming; Neutron Scattering; Einstein-Debye’s Breakdown; Cooperative Rearranging Region

  JOURNAL NAME: Open Journal of Biophysics, Vol.2 No.3, July 27, 2012

  ABSTRACT: Here we examine the findings obtained for disaccharide/water mixtures near glass transition that involves cooperative relaxation features on kinetic by viscosity and on thermodynamic behaviour by neutron scattering. Then to address cooperative phenomena that mitigate the Debye-Waller behaviour we invoke Adam-Gibbs’ idea of a cooperative rearranging region. Neutron results suggest that the excess mean square displacement behaves as free volume and is closely connected to an elementary step of the structural relaxation. Then viscosity data evidence a breakdown of the Einstein-Debye relation, decoupling attributed to the intermolecular cooperativity.