Protein recognition and dynamics in the early steps of aggregation (360G-Wellcome-089311_Z_09_Z)
In this study, we propose to use modern NMR and molecular dynamics (MD) simulations to investigate the dynamics of ?2m and to explore the role of further conformational changes of ?N6 in the early stages of protein aggregation. Specifically we aim to: 1. Study the dynamics of 132m in vitro, using NMR relaxation dispersion experiments, to understand the transition from the folded structure of t.N6 to species with enhanced amyloidogenic properties. 2. Use Paramagnetic Relaxation Enhancement (PRE) technique1s to characterise transient lowly populated dimerisation events that occur in the early stages of t.N6 aggregation. 3. Use molecular dynamics simulations to characterise local flexibility of l32m and expand our understanding of the amyloid formation pathway.
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Grant Details
| Amount Awarded | 142657 |
| Applicant Surname | Karamanos |
| Approval Committee | Molecules, Genes and Cells Funding Committee |
| Award Date | 2009-04-21T00:00:00+00:00 |
| Financial Year | 2008/09 |
| Grant Programme: Title | PhD Studentship (Basic) |
| Internal ID | 089311/Z/09/Z |
| Lead Applicant | Mr Theodoros Karamanos |
| Partnership Value | 142657 |
| Planned Dates: End Date | 2013-09-30T00:00:00+00:00 |
| Planned Dates: Start Date | 2009-10-01T00:00:00+00:00 |
| Recipient Org: Country | United Kingdom |
| Region | Yorkshire and the Humber |
| Sponsor(s) | Prof Alan Berry |