Complete assignment of the 1H NMR spectrum of a synthetic zinc finger from Xfin. Sequential resonance assignments and secondary structure.
FEBS Lett.1989 Aug 28;254(1-2):159-64
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摘要
A 25-residue synthetic peptide corresponding to zinc finger 31 of the Xenopus protein Xfin adopts a compact, folded conformation in the presence of zinc. Complete 1H resonance assignments have been made. The peptide contains a helix, beginning as an alpha-helix and ending as a 3(10)-helix, that extends from residue 12 to 23. Several positively charged and polar residues located on this helix are likely to be involved in interactions with DNA. Residues 1-10 appear to adopt a hairpin-like structure.
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基因功能
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原始数据
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文献解读
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