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Complete assignment of the 1 H NMR spectrum of a synthetic zinc finger from Xfin Sequential resonance assignments and secondary structure
Author(s) -
Lee Min S.,
Cavanagh John,
Wright Peter E.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81030-0
Subject(s) - zinc finger , helix (gastropod) , zinc , residue (chemistry) , chemistry , peptide , crystallography , protein secondary structure , stereochemistry , resonance (particle physics) , nuclear magnetic resonance spectroscopy , zinc finger nuclease , physics , biochemistry , biology , organic chemistry , ecology , particle physics , snail , transcription factor , gene
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 1 H resonance assignments have been made. The peptide contains a helix, beginning as an α‐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.