F
Flavio Toma
Researcher at French Alternative Energies and Atomic Energy Commission
Publications - 45
Citations - 1553
Flavio Toma is an academic researcher from French Alternative Energies and Atomic Energy Commission. The author has contributed to research in topics: Amino acid & Nuclear magnetic resonance spectroscopy. The author has an hindex of 19, co-authored 45 publications receiving 1535 citations.
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Refined structure of charybdotoxin: common motifs in scorpion toxins and insect defensins
TL;DR: A high-resolution model depicting the tertiary structure of Chtx, a blocker of K+ channels, has been obtained by DIANA and X-PLOR calculations from new proton nuclear magnetic resonance (NMR) data.
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Three‐dimensional structure of natural charybdotoxin in aqueous solution by 1H‐NMR Charybdotoxin possesses a structural motif found in other scorpion toxins
François Bontems,Christian Roumestand,Philippe Boyot,Bernard Gilquin,Yvon Doljansky,André Ménez,Flavio Toma +6 more
TL;DR: A 600-MHz proton NMR study of natural charybdotoxin, a toxin acting on K+ channels, is reported, showing that this structural motif is common to all these proteins.
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Scorpion toxins as natural scaffolds for protein engineering
TL;DR: The alpha/beta scorpion motif, small in size, easily amenable to chemical synthesis, highly stable, and tolerant for sequence mutations represents an appropriate scaffold onto which polypeptide sequences may be introduced in a predetermined conformation, providing an additional means for design and engineering of small proteins.
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Analysis of side-chain organization on a refined model of charybdotoxin: structural and functional implications.
TL;DR: This study shows, in fact, that functionally important positive residues are located on the helix side of the toxin, and charybdotoxin and scyllatoxin interact with two different classes of K+ channels by two different parts of the motif.
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Three-dimensional solution structure of a curaremimetic toxin from Naja nigricollis venom: a proton NMR and molecular modeling study.
Sophie Zinn-Justin,Christian Roumestand,Bernard Gilquin,François Bontems,André Ménez,Flavio Toma +5 more
TL;DR: The solution conformation of toxin alpha from Naja nigricollis, a snake toxin which specifically blocks the activity of the nicotinic acetylcholine receptor (AcChoR), has been determined using nuclear magnetic resonance spectroscopy and molecular modeling.