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Probing the exposure of tyrosine and tryptophan residues in partially folded proteins and folding intermediates by CIDNP pulse-labeling.

Abstract:

A nuclear magnetic resonance (NMR) technique has been devised to probe the structures of disordered, partially folded states of proteins at the level of individual amino acid residues. Chemically induced dynamic nuclear polarization (CIDNP) is first generated in exposed aromatic side-chains of the denatured state and then transferred to the high-resolution NMR spectrum of the native state by stimulating rapid refolding of the protein. Crucial improvements in sensitivity were achieved by carry...

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Publication status:
Published

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Publisher copy:
10.1021/ja020141w

Authors


Dobson, CM More by this author
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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Physical and Theoretical Chem
Journal:
Journal of the American Chemical Society
Volume:
124
Issue:
44
Pages:
13018-13024
Publication date:
2002-11-05
DOI:
EISSN:
1520-5126
ISSN:
0002-7863
URN:
uuid:dd6f845e-517b-4c69-8860-4cd7b1f9661f
Source identifiers:
32238
Local pid:
pubs:32238

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