The Role of Solvent in the Protein Dynamical Transition

Experimental and computer simulation studies have revealed the presence of a transition in the dynamics of hydrated proteins around 220 K. This transition has been compared with that of a glass phase transition. It manifests itself by a nonlinear behavior in the temperature dependence of the average atomic mean-square displacements and involves an increase of the amplitude of protein dynamics. This increase in flexibility has been correlated with the onset of protein activity. In this thesis, the mechanisms behind the protein dynamical transition are explored using molecular dynamics simulations and neutron scattering experiments.

Level thesis:degree_level

thesis.doctoral

Grantor dc:publisher

Universität Heidelberg

Year

2003

Author dc:creator

• Tournier, Alexander Louis

Contributors dc:contributor

• Smith, Jeremy

Repository record source_url

http://www.ub.uni-heidelberg.de/archiv/4377

OAI identifier oai:identifier

oai:archiv.ub.uni-heidelberg.de:4377