Structural Properties of the Putative Fusion Peptide of Fertilin, a Protein Active in Sperm−Egg Fusion, upon Interaction with the Lipid Bilayer†

Biochemistry ◽  
1998 ◽  
Vol 37 (48) ◽  
pp. 17030-17039 ◽  
Author(s):  
Isabelle Martin ◽  
Richard M. Epand ◽  
Jean-Marie Ruysschaert
Keyword(s):  
Structural Properties ◽  
Lipid Bilayer ◽  
Fusion Peptide

Dynamical and structural properties of charged and uncharged lidocaine in a lipid bilayer

2007 ◽  
Vol 125 (2-3) ◽  
pp. 416-424 ◽  
Author(s):  
Carl-Johan Högberg ◽  
Arnold Maliniak ◽  
Alexander P. Lyubartsev
Keyword(s):  
Structural Properties ◽  
Lipid Bilayer

scholarly journals Membrane Structures of the Hemifusion-Inducing Fusion Peptide Mutant G1S and theFusion-Blocking Mutant G1V of Influenza Virus HemagglutininSuggest a Mechanism for Pore Opening in MembraneFusion

2005 ◽  
Vol 79 (18) ◽  
pp. 12065-12076 ◽  
Author(s):  
Yinling Li ◽  
Xing Han ◽  
Alex L. Lai ◽  
John H. Bushweller ◽  
David S. Cafiso ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Membrane Fusion ◽  
Lipid Bilayer ◽  
Membrane Surface ◽  
Helical Structure ◽  
Fusion Peptide ◽  
Membrane Structures ◽  
Influenza Virus Hemagglutinin ◽  
Target Membrane ◽  
Pore Opening

ABSTRACT Influenza virus hemagglutinin (HA)-mediated membrane fusion is initiated by a conformational change that releases a V-shaped hydrophobic fusion domain, the fusion peptide, into the lipid bilayer of the target membrane. The most N-terminal residue of this domain, a glycine, is highly conserved and is particularly critical for HA function; G1S and G1V mutant HAs cause hemifusion and abolish fusion, respectively. We have determined the atomic resolution structures of the G1S and G1V mutant fusion domains in membrane environments. G1S forms a V with a disrupted “glycine edge” on its N-terminal arm and G1V adopts a slightly tilted linear helical structure in membranes. Abolishment of the kink in G1V results in reduced hydrophobic penetration of the lipid bilayer and an increased propensity to formβ -structures at the membrane surface. These results underline the functional importance of the kink in the fusion peptide and suggest a structural role for the N-terminal glycine ridge in viral membrane fusion.

scholarly journals Structural Properties of Membrane Inserted Fusion Peptide from Influenza Virus Analysed by Molecular Simulation

2014 ◽  
Vol 106 (2) ◽  
pp. 53a
Author(s):  
Diana Lousa ◽  
Bruno L. Victor ◽  
Carlos Fernandez ◽  
Cláudio M. Soares
Keyword(s):  
Influenza Virus ◽  
Structural Properties ◽  
Molecular Simulation ◽  
Fusion Peptide

scholarly journals Lysophosphatidylcholine mediates the mode of insertion of the NH2 -terminal SIV fusion peptide into the lipid bilayer

FEBS Letters ◽  
1993 ◽  
Vol 333 (3) ◽  
pp. 325-330 ◽  
Author(s):  
I. Martin ◽  
M.-C. Dubois ◽  
T. Saermark ◽  
R.M. Epand ◽  
J.-M. Ruysschaert
Keyword(s):  
Lipid Bilayer ◽  
Fusion Peptide

Fusion Peptide Interaction with Lipid Bilayer: Modeling with Monte Carlo Simulation and Continuum Electrostatics Calculation

2000 ◽  
Vol 24 (4-6) ◽  
pp. 341-349 ◽  
Author(s):  
Yuri A. Kosinsky ◽  
Peter V. Dubovskii ◽  
Dmitry E. Nolde ◽  
Alexander S. Arseniev ◽  
Roman G. Efremov
Keyword(s):  
Monte Carlo Simulation ◽  
Monte Carlo ◽  
Lipid Bilayer ◽  
Fusion Peptide ◽  
Continuum Electrostatics ◽  
Peptide Interaction

scholarly journals Hemagglutinin Fusion Peptide Mutants in Model Membranes: Structural Properties, Membrane Physical Properties, and PEG-Mediated Fusion

2011 ◽  
Vol 101 (5) ◽  
pp. 1095-1104 ◽  
Author(s):  
Md. Emdadul Haque ◽  
Hirak Chakraborty ◽  
Tilen Koklic ◽  
Hiroaki Komatsu ◽  
Paul H. Axelsen ◽  
...  
Keyword(s):  
Physical Properties ◽  
Structural Properties ◽  
Fusion Peptide ◽  
Model Membranes
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