Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractNMR analysis of the conformations of membrane-bound peptides    Next AbstractConformations of yeast alpha-mating factor and analog peptides as bound to phospholipid bilayer. Correlation of membrane-bound conformation with physiological activity »

Eur J Biochem


Title:Nuclear-magnetic-resonance studies on the conformation of membrane-bound alpha-mating factor. Transferred nuclear Overhauser effect analysis
Author(s):Wakamatsu K; Okada A; Suzuki M; Higashijima T; Masui Y; Sakakibara S; Miyazawa T;
Address:
Journal Title:Eur J Biochem
Year:1986
Volume:154
Issue:3
Page Number:607 - 615
DOI: 10.1111/j.1432-1033.1986.tb09442.x
ISSN/ISBN:0014-2956 (Print) 0014-2956 (Linking)
Abstract:"The C-H proton resonances of alpha-mating factor, yeast pheromone, in 2H2O solution were assigned. The phase transition temperature of perdeuterated dipalmitoylglycerophosphocholine (suspension) was found to be 35.5 degrees C. In the presence of vesicles of this phospholipid, the exchange broadening and transferred nuclear Overhauser effect (TRNOE) of peptide proton resonances (at 50 degrees C) were analyzed. The mode of binding of this peptide with the phospholipid bilayer was elucidated. The N-terminal nine residues (Trp1-Gly9) are tightly bound to the bilayer, while the C-terminal four residues (Gln10-Tyr13) are left free in aqueous phase. This is consistent with the previous observation that the C-terminal three residues (Pro11-Tyr13) are not essential for the activity of this pheromone [Masui, Y. et al. (1977) Biochem. Biophys. Res. Commun. 78, 534-538]. Furthermore, from the TRNOE analyses, the conformation of the membrane-bound N-terminal part of alpha-mating factor was elucidated; the residues Trp1-Gln5 form a compact helical structure while the residues Lys7-Gly9 form an extended structure. A similar TRNOE was also observed for an active decapeptide analog Trp1-Gln10. This confirms the previous conclusion that the physiological activities of this pheromone and analog peptides are correlated with the conformations of membrane-bound peptide molecules [Higashijima, T. et al. (1983) FEBS Lett. 159, 229-232]"
Keywords:*Fungal Proteins Magnetic Resonance Spectroscopy Mating Factor Membrane Proteins Peptide Fragments *Peptides Phosphatidylcholines Protein Conformation Saccharomyces cerevisiae Temperature;
Notes:"MedlineWakamatsu, K Okada, A Suzuki, M Higashijima, T Masui, Y Sakakibara, S Miyazawa, T eng Research Support, Non-U.S. Gov't England 1986/02/03 Eur J Biochem. 1986 Feb 3; 154(3):607-15. doi: 10.1111/j.1432-1033.1986.tb09442.x"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 22-11-2024