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Old 08-02-2011, 11:40 AM
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Default NMR studies of the solution conformation of the sex peptide from Drosophila melanogaster.

NMR studies of the solution conformation of the sex peptide from Drosophila melanogaster.

NMR studies of the solution conformation of the sex peptide from Drosophila melanogaster.

FEBS Lett. 2011 Apr 20;585(8):1197-202

Authors: Moehle K, Freund A, Kubli E, Robinson JA

The insect sex peptide (SP) elicits a variety of biological responses upon transfer to the mated female. SP contains 36 amino acids, including a tryptophan-rich N-terminal region, a central region containing five hydroxyproline (Hyp) residues, and a C-terminal region enclosed by a disulfide bridge. The solution structure of SP, studied here using NMR spectroscopy, includes a motif WPWN that adopts a type I ?-turn in the N-terminal Trp-rich region. This turn region is connected to the central Hyp-rich region, which adopts extended and/or PPII-like conformations. The C-terminal disulfide-bonded loop populates helical turns or nascent helical structure. Overall, the results reveal a rather flexible peptide that lacks a compact folded structure in solution.

PMID: 21439282 [PubMed - indexed for MEDLINE]



Source: PubMed
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