The molecular biophysics of enhanced enzyme stability in extreme environments

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Project objective

Research objectives and content Enzymes from certain organisms are adapted to function in extreme environments, e.g. thermophiles and halophiles. As protein-solvent interactions play a major role in controlling enzyme stability and function, I propose a study of how these solvent interactions are modulated both by the sequence changes found in these enzymes and also in modified solvents in which they retain their activity under extreme conditions. By performing atomic level computer simulations on both normal and cryosolvent solutions of mesophilic and thermophilic xylanase enzymes (being used in parallel experimental study at the host laboratory), I propose to explore the influence of the temperature and the solvent on the protein-solvent interactions in these systems The results of this work are expected to improve our understanding of the influence of the forces leading to enhanced thermal stability of thermophilic enzymes, and give new insights into the molecular mechanisms of cryopreservation of biological materials. Training content (objective, benefit and expected impact) The work programme will enable me to build up new expertise in the increasingly important techniques of computer simulation of protein structure-dynamics-function. Involvement with the experimental work will also exploit and further develop my experimental abilities in neutron studies of protein dynamics that were gained during my Ph.D. work.

Original text from CORDIS.

Participants

• UNIVERSITY COLLEGE LONDON · LONDONCoordinatorUnited Kingdom
• Not availableCity levelFrance

Links

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