Fernando Formaggio focuses on Stereochemistry, Peptide, Crystallography, Amino acid and Circular dichroism. His Stereochemistry research is multidisciplinary, incorporating elements of Residue, Helix, Fourier transform, Protein structure and Oligopeptide. His biological study spans a wide range of topics, including 310 helix, Membrane and Solvent.
His studies deal with areas such as Proton NMR, Electron paramagnetic resonance, Spin label, Nuclear magnetic resonance spectroscopy and Molecule as well as Crystallography. His research in Amino acid intersects with topics in Collagen helix and Polymer chemistry. His study in the field of Vibrational circular dichroism is also linked to topics like Histone octamer.
His primary areas of investigation include Stereochemistry, Peptide, Crystallography, Amino acid and Residue. His research in Stereochemistry is mostly concerned with Circular dichroism. The study incorporates disciplines such as Combinatorial chemistry, Side chain, Membrane and Protein secondary structure in addition to Peptide.
In his research on the topic of Crystallography, Hydrogen bond is strongly related with Intramolecular force. His Amino acid study often links to related topics such as Random hexamer. His biological study deals with issues like Tripeptide, which deal with fields such as Tetrapeptide.
Fernando Formaggio mainly investigates Peptide, Stereochemistry, Crystallography, Electron paramagnetic resonance and Membrane. The Peptide study combines topics in areas such as Molecular dynamics, Covalent bond, Helix, Molecule and Combinatorial chemistry. His Stereochemistry research is multidisciplinary, relying on both Residue, Amino acid, Peptide bond and Peptide Conformation.
In his study, Chromophore and Conformational isomerism is strongly linked to Fluorescence, which falls under the umbrella field of Crystallography. In general Electron paramagnetic resonance, his work in Spin label is often linked to Nitroxide mediated radical polymerization linking many areas of study. His research integrates issues of Biological activity, Nitroxyl, Cytotoxicity and Antimicrobial peptides in his study of Membrane.
Fernando Formaggio mainly focuses on Stereochemistry, Peptide, Crystallography, Peptide Conformation and Helix. The various areas that Fernando Formaggio examines in his Stereochemistry study include Amino acid, Molecular dynamics, Residue, Conformational isomerism and Peptidomimetic. His studies in Conformational isomerism integrate themes in fields like Liposome and Circular dichroism.
His Peptide research incorporates elements of Fibril, Fluorescence, Electron transfer, Protein structure and Side chain. His Crystallography research integrates issues from Molecule and Resonance. His Helix study deals with X-ray crystallography intersecting with Density functional theory, Structural biology, Coupling reaction and Infrared spectroscopy.
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Control of peptide conformation by the Thorpe-Ingold effect (C alpha-tetrasubstitution).
Claudio Toniolo;Marco Crisma;Fernando Formaggio;Cristina Peggion.
Biopolymers (2001)
Circular Dichroism Spectrum of a Peptide 310-Helix
Claudio Toniolo;Alessandra Polese;Fernando Formaggio;Marco Crisma.
Journal of the American Chemical Society (1996)
Structures of peptides from alpha-amino acids methylated at the alpha-carbon.
C Toniolo;M Crisma;F Formaggio;G Valle.
Biopolymers (1993)
Conformational Characterization of Terminally Blocked l-(αMe)Val Homopeptides Using Vibrational and Electronic Circular Dichroism. 310-Helical Stabilization by Peptide−Peptide Interaction
Gorm Yoder;Alessandra Polese;R. A. G. D. Silva;Fernando Formaggio.
Journal of the American Chemical Society (1997)
Dinuclear Zn(2+) complexes of synthetic heptapeptides as artificial nucleases.
Claudia Sissi;Paola Rossi;Fulvia Felluga;Fernando Formaggio.
Journal of the American Chemical Society (2001)
Lipopeptaibols, a novel family of membrane active, antimicrobial peptides.
C Toniolo;M Crisma;F Formaggio;C Peggion.
Cellular and Molecular Life Sciences (2001)
Structure determination of racemic trichogin A IV using centrosymmetric crystals
Claudio Toniolo;Cristina Peggion;Marco Crisma;Fernando Formaggio.
Nature Structural & Molecular Biology (1994)
Peptide helices based on α‐amino acids
Marco Crisma;Fernando Formaggio;Alessandro Moretto;Claudio Toniolo.
Biopolymers (2006)
ESR Characterization of Hexameric, Helical Peptides Using Double TOAC Spin Labeling
Paul Hanson;Glenn Millhauser;Fernando Formaggio;Marco Crisma.
Journal of the American Chemical Society (1996)
TOAC, a nitroxide spin‐labeled, achiral Cα‐tetrasubstituted α‐amino acid, is an excellent tool in material science and biochemistry
Claudio Toniolo;Marco Crisma;Fernando Formaggio.
Biopolymers (1998)
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