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Assignment of the backbone 1 H, 15 N, 13 C NMR resonances and secondary structure of a double‐stranded RNA binding domain from the Drosophila protein staufen
Author(s) -
Bycroft Mark,
Proctor Mark,
Freund Stefan M.V.,
Johnston Daniel St.
Publication year - 1995
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(95)00181-8
Subject(s) - chemistry , crystallography , rna , physics , gene , biochemistry
NMR spectroscopy has been used to determine the secondary structure of one of the double‐stranded RNA binding domains from the Drosophila protein staufen. The domain has an αβββα arrangement of secondary structure, with the β strands forming an antiparallel β sheet. The secondary structure differs from that found in the RNP RNA binding domain.