2012 - Fellow of the Australian Academy of Science
The scientist’s investigation covers issues in Biochemistry, Lipid bilayer, Membrane, Peptide and Bilayer. Her Lipid bilayer study combines topics from a wide range of disciplines, such as Crystallography, Vesicle, Biophysics and Membrane lipids. Her Crystallography research incorporates themes from Nuclear magnetic resonance spectroscopy, Solid-state nuclear magnetic resonance and Gramicidin.
Frances Separovic combines subjects such as Lysis, Quartz crystal microbalance and Protein secondary structure with her study of Membrane. Her research in Peptide intersects with topics in P3 peptide, POPC, Stereochemistry, Circular dichroism and Methionine. Frances Separovic focuses mostly in the field of Bilayer, narrowing it down to matters related to Molecule and, in some cases, Lipid bilayer mechanics, Head, Hydrocarbon, Chemical physics and Hexane.
Her primary areas of investigation include Peptide, Membrane, Biochemistry, Lipid bilayer and Biophysics. Her biological study deals with issues like Stereochemistry, which deal with fields such as Gramicidin. Her research integrates issues of Solid-state nuclear magnetic resonance and Protein secondary structure in her study of Membrane.
Her Biochemistry study frequently draws parallels with other fields, such as P3 peptide. Her Lipid bilayer study combines topics in areas such as Crystallography, Vesicle, Bilayer and Membrane lipids. While the research belongs to areas of Crystallography, she spends her time largely on the problem of Nuclear magnetic resonance spectroscopy, intersecting her research to questions surrounding Carbon-13 NMR.
Her main research concerns Peptide, Biochemistry, Membrane, Antimicrobial peptides and Biophysics. Her studies deal with areas such as Receptor, Antimicrobial and Stereochemistry, Circular dichroism as well as Peptide. Her Biochemistry research includes themes of Bacterial outer membrane and Staphylococcus aureus.
Her research investigates the connection between Membrane and topics such as Solid-state nuclear magnetic resonance that intersect with issues in Combinatorial chemistry. In Antimicrobial peptides, Frances Separovic works on issues like Nuclear magnetic resonance spectroscopy, which are connected to Molecular dynamics. Her work on Model lipid bilayer as part of her general Lipid bilayer study is frequently connected to Pore-forming toxin, thereby bridging the divide between different branches of science.
Her scientific interests lie mostly in Peptide, Biochemistry, Membrane, Antimicrobial peptides and Biophysics. Her Peptide research includes elements of Agonist, Amino acid, Small molecule and Cytotoxicity. Her Biochemistry research is multidisciplinary, incorporating elements of Dimer and Monomer.
Her study in Membrane focuses on Cell membrane in particular. Her Antimicrobial peptides research is multidisciplinary, relying on both Nuclear magnetic resonance spectroscopy and Lipid bilayer. Her studies in Biophysics integrate themes in fields like Melittin, Sphingomyelin, Vesicle, Bilayer and Micelle.
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29Si NMR study of structural ordering in aluminosilicate geopolymer gels.
Peter Duxson;John L. Provis;Grant C. Lukey;Frances Separovic.
Interfacial Anchor Properties of Tryptophan Residues in Transmembrane Peptides Can Dominate over Hydrophobic Matching Effects in Peptide−Lipid Interactions†
M.R.R. de Planque;B.B. Bonev;J.A.A. Demmers;D.V. Greathouse.
How Membrane-Active Peptides Get into Lipid Membranes.
Marc-Antoine Sani;Frances Separovic.
Accounts of Chemical Research (2016)
Electrochemistry of Room Temperature Protic Ionic Liquids
Chuan Zhao;Geoffrey Burrell;Angel Alberto Jesus Torriero;Frances Separovic.
Journal of Physical Chemistry B (2008)
Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance.
Margit A. Apponyi;Tara L. Pukala;Craig S. Brinkworth;Vita M. Maselli.
Direct visualization of membrane leakage induced by the antibiotic peptides: maculatin, citropin, and aurein.
Ernesto E. Ambroggio;Frances Separovic;John H. Bowie;Gerardo D. Fidelio.
Biophysical Journal (2005)
Neurotoxic, Redox-competent Alzheimer's β-Amyloid Is Released from Lipid Membrane by Methionine Oxidation
Kevin J. Barnham;Giuseppe D. Ciccotosto;Anna K. Tickler;Anna K. Tickler;Feda E. Ali.
Journal of Biological Chemistry (2003)
Implications of peptide assemblies in amyloid diseases
Pu Chun Ke;Marc Antonie Sani;Feng Ding;Aleksandr Kakinen.
Chemical Society Reviews (2017)
Copper-mediated amyloid-beta toxicity is associated with an intermolecular histidine bridge
D P Smith;D P Smith;Danielle G Smith;Danielle G Smith;Cyril C Curtain;Cyril C Curtain;Cyril C Curtain;John Frank Boas.
Journal of Biological Chemistry (2006)
Surface Behavior and Lipid Interaction of Alzheimer β-Amyloid Peptide 1–42: A Membrane-Disrupting Peptide
Ernesto E. Ambroggio;Dennis H. Kim;Frances Separovic;Colin J. Barrow.
Biophysical Journal (2005)
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