期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 133, 期 32, 页码 12370-12373出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja204062v
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资金
- National Institutes of Health [5R01GM081793-03, 5DP1OD783]
- NSF [MCB 1051819, DMR-0654118]
- Penn State University College of Medicine
- National Natural Science Foundation of China [21075134]
- State of Florida
- U.S. Department of Energy
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1051819] Funding Source: National Science Foundation
The feasibility of using solid-state magic-angle-spinning NMR spectroscopy for in situ structural characterization of the LR11 (sorLA) transmembrane domain (TM) in native Escherichia coli membranes is presented. LR11 interacts with the human amyloid precursor protein (APP), a central player in the pathology of Alzheimer's disease. The background signals from E. coli lipids and membrane proteins had only minor effects on the LR11 TM resonances. Approximately 50% of the LR11 TM residues were assigned by using C-13 PARIS data. These assignments allowed comparisons of the secondary structure of the LR11 TM in native membrane environments and commonly used membrane mimics (e.g., micelles). In situ spectroscopy bypasses several obstacles in the preparation of membrane proteins for structural analysis and offers the opportunity to investigate how membrane heterogeneity, bilayer asymmetry, chemical gradients, and macromolecular crowding affect the protein structure.
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