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NMR assignments of PI3-SH3 domain aided by protonless NMR spectroscopy |
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| Authors: | Shang-Te Danny Hsu |
| Affiliation: | 1. Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK 2. Institute of Biological Chemistry, Academia Sinica, 128, Section?2, Academia Road, Taipei, 11529, Taiwan 3. Institute of Biochemical Sciences, National Taiwan University, 1, Section?2, Roosevelt Road, Taipei, 10617, Taiwan 4. Institute of Bioinformatics and Structural Biology, National Tsing Hua University, 101, Section?2, Kuang-Fu Road, Hsinchu, 30013, Taiwan |
| Abstract: | We report here the near complete assignments of native bovine PI3-SH3 domain, which has been a model system for protein folding, misfolding and amyloid fibril formation. The use of 13C-detected protonless NMR spectroscopy is instrumental in assigning the spin system of the proline residue at the C-terminus in addition to the missing resonances in proton-based NMR spectra due to rapid solvent exchange. It also helps assign the resonances of all three proline amine nitrogen nuclei, which are underrepresented in the database. Comparison of the backbone 13C resonances of PI3-SH3 in its native and amyloid fibril states shows that the aggregation of PI3-SH3 is accompanied by major conformational rearrangements. |
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