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- E-ISSN 2288-8985
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Structural Studies of Membrane Protein by Solid-state NMR Spectroscopy
Analytical Science and Technology / Analytical Science and Technology, (P)1225-0163; (E)2288-8985
2004, v.17 no.5, pp.388-392
(2004). Structural Studies of Membrane Protein by Solid-state NMR Spectroscopy. Analytical Science and Technology, 17(5), 388-392.
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Abstract
Structural studies of membrane proteins, importantly involving interpretation of genomics information, many signaling pathway and major drug target for drug discovery, are having difficulty in characterizing the function using conventional solution nmr spectroscopy and x-ray crystallography because phospholipid bilayers hindered fast tumbling and crystallization. Here, we studied the structure of the pf1 coat protein in oriented phospholipid bilayers by home-built solid-state NMR probe. Bacteriophage pf1 was purified from Paeudomonas Aeruginosa and coat protein of bacteriophage pf1 was isolated from DNA and other proteins.
- keywords
- Membrane protein, Solid-state NMR, Home-built solid-state NMR probe, Bacteriophage pf1 coat protein, protein purification
Reference
1
Y Kim, (1994) Methods in Enzymology 239,
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