Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 132, Issue 43, Pages 15164-15166Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja107460j
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Funding
- Max Planck Society
- DFG
- Fondation Bettencourt Schueller
- European Molecular Biology Organization
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We present a robust solid-state NMR approach for the accurate determination of molecular interfaces in insoluble and noncrystalline protein protein complexes. The method relies on the measurement of intermolecular C-13-C-13 distances in mixtures of [1-C-13]glucose- and [2-C-13]glucose-labeled proteins. We have applied this method to Parkinson's disease-associated a-synuclein fibrils and found that they are stacked in a parallel in-register arrangement. Additionally, intermolecular distance restraints for the structure determination of the fibrils at atomic resolution were measured.
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