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. 1992 May 15;89(10):4397–4401. doi: 10.1073/pnas.89.10.4397

Complete 15N and 1H NMR assignments for the amino-terminal domain of the phage 434 repressor in the urea-unfolded form

Dario Neri 1, Gerhard Wider 1, Kurt Wüthrich 1
PMCID: PMC49089  PMID: 1584772

Abstract

The amino-terminal domain of the phage 434 repressor consisting of residues 1-69 forms a globular structure of five tightly packed helices, with nearly identical molecular architectures in crystals and in solution. Upon addition of urea to an aqueous solution of this protein, the NMR spectrum of a second form of the protein appears in addition to the native form, and at a urea concentration of 7 M, this urea-unfolded form is the only species observed. At intermediate urea concentrations, the two forms of the protein inter-convert at a rate that allows the observation of the exchange process by NMR. Starting from the previous assignments for the native protein, we obtained nearly complete sequence-specific 1H and 15N NMR assignments for the unfolded form of the protein. For most amino acid residues, the 1H chemical shifts of the urea-unfolded protein are very similar to the random coil values, but some discrete regions of the polypeptide chain were identified that are likely to retain residual nonrandom spatial structure as evidenced by deviations of 1H chemical shifts and amide proton exchange rates from the expected random coil values.

Keywords: sequence-specific NMR assignments, protein denaturation, protein folding, isotope-labeled proteins

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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