Abstract
Photocleavage of the polypeptide backbone is potentially a powerful and general method to activate or deactivate functional peptides and proteins with high spatial and temporal resolution. Here we show that 2-nitrophenylalanine is able to photochemically cleave the polypeptide backbone by an unusual cinnoline-forming reaction. This unnatural amino acid was genetically encoded in E. coli, and protein containing 2-nitrophenylalanine was expressed and site-specifically photocleaved.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Amino Acid Substitution
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Bacteriophage T4 / enzymology
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Bacteriophage T4 / genetics
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Escherichia coli / genetics
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Muramidase / chemistry
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Muramidase / genetics
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Muramidase / metabolism
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Peptides / chemistry
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Peptides / metabolism
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Phenylalanine / analogs & derivatives*
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Phenylalanine / genetics
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Phenylalanine / metabolism
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Photochemistry
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Protein Engineering
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Proteins / chemistry
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Proteins / genetics*
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Proteins / metabolism*
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Viral Proteins / chemistry
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Viral Proteins / genetics
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Viral Proteins / metabolism
Substances
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2-nitrophenylalanine
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Peptides
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Proteins
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Viral Proteins
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Phenylalanine
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Muramidase