Understanding the folding, misfolding, and polymerization of a1-antitrypsin using NMR spectroscopy (360G-Wellcome-090556_Z_09_Z)
A. Assess the structural and dynamical characteristics of the native state of a1-antitrypsin at a residue specific level using NMR spectroscopy and mass spectrometry. B. Using NMR spectroscopy, examine the folding pathway of AAT at a residue specific level and structurally characterize partially folded intermediate states that are formed during this process. C. Understand the folding of AA T as it occurs during synthesis, by examining ribosome bound nascent chains of AAT using NMR spectroscopy and biophysics. D. Assess the structure of the ?1-antitrypsin end-points of folding: latent, polymer; using the wildtype ?1-antitrypsin in polymerization condition, and the most common mutation of serpins: Z ?1-antitrypsin, determined by NMR.
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Grant Details
| Amount Awarded | 152244 |
| Applicant Surname | Levy |
| Approval Committee | Molecules, Genes and Cells Funding Committee |
| Award Date | 2009-08-31T00:00:00+00:00 |
| Financial Year | 2008/09 |
| Grant Programme: Title | PhD Studentship (Basic) |
| Internal ID | 090556/Z/09/Z |
| Lead Applicant | Ms Geraldine Levy |
| Partnership Value | 152244 |
| Planned Dates: End Date | 2013-09-27T00:00:00+00:00 |
| Planned Dates: Start Date | 2009-09-28T00:00:00+00:00 |
| Recipient Org: Country | United Kingdom |
| Region | Greater London |
| Sponsor(s) | Prof Gabriel Waksman |