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

Moehle, K; Freund, A; Kubli, E; Robinson, J A (2011). NMR studies of the solution conformation of the sex peptide from Drosophila melanogaster. FEBS Letters, 585(8):1197-1202.

Abstract

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 β-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.

Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:07 Faculty of Science > Department of Chemistry
Dewey Decimal Classification:540 Chemistry
Scopus Subject Areas:Life Sciences > Biophysics
Life Sciences > Structural Biology
Life Sciences > Biochemistry
Life Sciences > Molecular Biology
Life Sciences > Genetics
Life Sciences > Cell Biology
Language:English
Date:2011
Deposited On:09 Jan 2012 16:10
Last Modified:06 Nov 2024 02:39
Publisher:Elsevier
ISSN:0014-5793
OA Status:Green
Publisher DOI:https://doi.org/10.1016/j.febslet.2011.03.040
PubMed ID:21439282
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  • Language: English
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