His scientific interests lie mostly in Peptide, Stereochemistry, Ion, Mass spectrum and Biochemistry. His research integrates issues of Protein secondary structure, Peptide sequence, Nuclear magnetic resonance spectroscopy, Membrane and Tree frog in his study of Peptide. His Stereochemistry research includes themes of Protein structure, Amino acid, Deprotonation and Alkyl.
His Ion research is multidisciplinary, incorporating perspectives in Chemical physics, Computational chemistry and Mass spectrometry. His Mass spectrum study combines topics from a wide range of disciplines, such as Deuterium, Oxazole, Ring and Medicinal chemistry. His work in the fields of Antimicrobial peptides, Neuropeptide, Nitric oxide synthase and Secretion overlaps with other areas such as Mechanism of action.
John H. Bowie mostly deals with Ion, Medicinal chemistry, Mass spectrum, Stereochemistry and Deprotonation. The concepts of his Ion study are interwoven with issues in Photochemistry and Mass spectrometry, Analytical chemistry. His Medicinal chemistry study incorporates themes from Deuterium, Aryl, Alkyl and Yield.
In his research, Singlet state and Molecule is intimately related to Crystallography, which falls under the overarching field of Mass spectrum. His Stereochemistry research focuses on Peptide and how it connects with Peptide sequence, Tree frog, Amino acid and Chromatography. His Deprotonation research incorporates elements of Aliphatic compound and Wittig reaction.
John H. Bowie mainly focuses on Peptide, Ion, Stereochemistry, Mass spectrometry and Biochemistry. His Peptide research integrates issues from Biophysics, Neuropeptide, Peptide sequence, Chromatography and Tree frog. He studies Mass spectrum, a branch of Ion.
His work deals with themes such as Fragmentation, Organic chemistry, Deprotonation and Hydrogen bond, which intersect with Stereochemistry. His studies deal with areas such as Ion source, Photochemistry and Physical chemistry as well as Mass spectrometry. The Antimicrobial peptides, Calmodulin and Protein secondary structure research John H. Bowie does as part of his general Biochemistry study is frequently linked to other disciplines of science, such as Mechanism of action, therefore creating a link between diverse domains of science.
John H. Bowie spends much of his time researching Peptide, Biochemistry, Stereochemistry, Antimicrobial peptides and Peptide sequence. His Peptide research is multidisciplinary, relying on both Electrospray mass spectrometry, Chromatography, Mass spectrometry and Antibacterial activity. His Membrane, Lipid bilayer and Venom study in the realm of Biochemistry interacts with subjects such as Mechanism of action.
His Stereochemistry research includes elements of Ion and Protein structure. In general Ion, his work in Mass spectrum is often linked to Thymine linking many areas of study. His study in Peptide sequence is interdisciplinary in nature, drawing from both Neuropeptide and Cyclorana.
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A novel method for the release and collection of dermal, glandular secretions from the skin of frogs.
Michael J. Tyler;David J.M. Stone;John H. Bowie.
Journal of Pharmacological and Toxicological Methods (1992)
The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2.
Tomas Rozek;Kate L. Wegener;John H. Bowie;Ian N. Olver.
FEBS Journal (2000)
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)
The fragmentations of even‐electron organic negative ions
John H. Bowie.
Mass Spectrometry Reviews (1990)
Antimicrobial Peptides from Amphibian Skin Potently Inhibit Human Immunodeficiency Virus Infection and Transfer of Virus from Dendritic Cells to T Cells
Scott E. VanCompernolle;R. Jeffery Taylor;Kyra Oswald-Richter;Jiyang Jiang.
Journal of Virology (2005)
The formation and fragmentation of negative ions derived from organic molecules
J. H. Bowie.
Mass Spectrometry Reviews (1984)
Interaction of antimicrobial peptides from Australian amphibians with lipid membranes.
Isabelle Marcotte;Kate L. Wegener;Yuen-Han Lam;Brian C.S. Chia.
Chemistry and Physics of Lipids (2003)
The Solution Structure and Activity of Caerin 1.1, an Antimicrobial Peptide from the Australian Green Tree Frog, Litoria Splendida
Herbert Wong;John H. Bowie;John A. Carver.
FEBS Journal (1997)
Gas phase acidities of the α amino acids
Richard A.J. O'Hair;John H. Bowie;Scott Gronert.
International Journal of Mass Spectrometry and Ion Processes (1992)
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