| EPSRC Reference: |
GR/R57393/01 |
| Title: |
Determination of Protein Structure During Microwave Irradation By In Situ X-Ray Diffraction. |
| Principal Investigator: |
Sawyer, Professor L |
| Other Investigators: |
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| Researcher Co-Investigators: |
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| Project Partners: |
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| Department: |
Inst of Cell and Molecular Biology |
| Organisation: |
University of Edinburgh |
| Scheme: |
Postdoctoral Mobility PreFEC |
| Starts: |
17 November 2001 |
Ends: |
16 November 2002 |
Value (£): |
61,151
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| EPSRC Research Topic Classifications: |
| Biological & Medicinal Chem. |
Chemical Biology |
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| EPSRC Industrial Sector Classifications: |
| Chemicals |
Communications |
| Energy |
No relevance to Underpinning Sectors |
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Summary on Grant Application Form |
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This proposal wishes to address the problem of understanding the structural changes that occur when molecules (especially macromolecules) are exposed to microwave radiation. It is already known that microwaves may enhance the rate of folding and unfolding of proteins, and functions such as gene expression may also be altered. However it is not understood precisely what structural changes take place as a result of such irradiation, and our knowledge of the functional implications of such changes is very limited. We propose to design and construct apparatus capable of irradiating a single crystal of a molecular material with microwaves whilst determining the structure by X-ray crystallography. We propose first to test this apparatus on relatively simple molecular materials, both to understand how microwaves perturb their structure, and also to test and perhaps modify the apparatus. We propose then to apply the technique to more complex molecular systems, for example the model protein beta-lactoglobulin, to gain insight into the modes that are excited by the radiation through a study of the spatial correlation of enhanced atomic thermal parameters. Such measurements would be complemented by theoretical (protein force field) calculations to relate such modes to folding/unfolding transition in the protein.
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Key Findings |
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This information can now be found on Gateway to Research (GtR) http://gtr.rcuk.ac.uk
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Potential use in non-academic contexts |
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This information can now be found on Gateway to Research (GtR) http://gtr.rcuk.ac.uk
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Impacts |
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| Description |
This information can now be found on Gateway to Research (GtR) http://gtr.rcuk.ac.uk |
| Summary |
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| Date Materialised |
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Sectors submitted by the Researcher |
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This information can now be found on Gateway to Research (GtR) http://gtr.rcuk.ac.uk
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| Project URL: |
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| Further Information: |
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| Organisation Website: |
http://www.ed.ac.uk |