• Analytical Science and Technology
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• v.17 no.5
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• pp.388-392
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• 2004

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.

• Journal of The Korean Radiological Technologist Association
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• v.25 no.1
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• pp.113-113
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• 1999

• Proceedings of the Korean Society of Tobacco Science Conference
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• 1998.05a
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• pp.23-24
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• 1998

• Proceedings of the Korean Society of Tobacco Science Conference
• /
• 1998.05a
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• pp.25-25
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• 1998

• Optical Science and Technology
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• v.8 no.4
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• pp.26-29
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• 2004

• Bulletin of Food Technology
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• v.3 no.3
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• pp.109-122
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• 1990

• Proceedings of the Korean Society of Radiological Science
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• 2002.06b
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• pp.32.3-32.3
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• 2002

• The Science & Technology
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• v.27 no.10 s.305
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• pp.66-67
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• 1994

• Polymer Science and Technology
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• v.24 no.6
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• pp.612-617
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• 2013

• Proceedings of the Korean Society of Postharvest Science and Technology of Agricultural Products Conference
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• 1994.07a
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• pp.21-21
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• 1994