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19F NMR studies of the native and denatured states of green fluorescent protein.

Abstract:

Biosynthetic preparation and (19)F NMR experiments on uniformly 3-fluorotyrosine-labeled green fluorescent protein (GFP) are described. The (19)F NMR signals of all 10 fluorotyrosines are resolved in the protein spectrum with signals spread over 10 ppm. Each tyrosine in GFP was mutated in turn to phenylalanine. The spectra of the Tyr --> Phe mutants, in conjunction with relaxation data and results from (19)F photo-CIDNP (chemically induced dynamic nuclear polarization) experiments, yielded...

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Publication status:
Published

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Publisher copy:
10.1021/ja060618u

Authors


Craggs, TD More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Physical and Theoretical Chem
Jackson, SE More by this author
Journal:
Journal of the American Chemical Society
Volume:
128
Issue:
33
Pages:
10729-10737
Publication date:
2006-08-05
DOI:
EISSN:
1520-5126
ISSN:
0002-7863
URN:
uuid:d4ed1e62-6594-4f85-8e89-dea2f5263977
Source identifiers:
33578
Local pid:
pubs:33578

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