期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 123, 期 37, 页码 8895-8901出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja0112846
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资金
- NIGMS NIH HHS [GM 56531-02, GM 08284] Funding Source: Medline
Our recently developed in-cell NMR procedure now enables one to observe protein conformations inside living cells. Optimization of the technique demonstrates that distinguishing the signals produced by a single protein species depends critically on protein overexpression levels and the correlation time in the cytoplasm. Less relevant is the selective incorporation of N-15. Poorly expressed proteins, insoluble proteins, and proteins that cannot tumble freely due to associations within the cell cannot yet be observed. We show in-cell NMR spectra of bacterial NmerA and human calmodulin and discuss limitations of the technique as well as prospects for future applications.
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