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

Journal article

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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Authors: Lyon, C; Suh, E; Dobson, C; Hore, P

• Publication status: Published
• Journal: Journal of the American Chemical Society
• Volume: 124
• Issue: 44
• Pages: 13018-13024
• Publication date: 2002-11-01
• DOI: 10.1021/ja020141w
• EISSN: 1520-5126
• ISSN: 0002-7863
• Language: English
• Keywords: Nuclear Magnetic Resonance, Biomolecular; Tyrosine; Lactalbumin; Muramidase; Photochemistry; Protein Folding; Tryptophan; Protein Denaturation