ISSN:
1573-5001
Keywords:
Zinc finger
;
2D NMR
;
Secondary structure
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Summary Essentially complete assignments have been obtained for the1H and protonated13C NMR spectra of the zinc finger peptide Xfin-31 in the presence and absence of zinc. The patterns observed for the1H and13C chemical shifts of the peptide in the presence of zinc, relative to the shifts in the absence of zinc, reflect the zinc-mediated folding of the unstructured peptide into a compact globular structure with distinct elements of secondary structure. Chemical shifts calculated from the 3D solution structure of the peptide in the presence of zinc and the observed shifts agree to within ca. 0.2 and 0.6 ppm for the backbone CaH and NH protons, respectively. In addition, homologous zinc finger proteins exhibit similar correlations between their1H chemical shifts and secondary structure.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01874810
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