http://www.cnr.it/ontology/cnr/individuo/prodotto/ID14654
Spatial distribution of spin-labeled trichogin GA IV in the Gram-positive bacterial cell membrane determined from PELDOR data (Articolo in rivista)
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- Spatial distribution of spin-labeled trichogin GA IV in the Gram-positive bacterial cell membrane determined from PELDOR data (Articolo in rivista) (literal)
- Anno
- 2002-01-01T00:00:00+01:00 (literal)
- Alternative label
Milov A.D., Samoilova R.I., Tsvetkov Yu.D., Gusev V.A., Formaggio F., Crisma M., Toniolo C., Raap J. (2002)
Spatial distribution of spin-labeled trichogin GA IV in the Gram-positive bacterial cell membrane determined from PELDOR data
in Applied magnetic resonance
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- Milov A.D., Samoilova R.I., Tsvetkov Yu.D., Gusev V.A., Formaggio F., Crisma M., Toniolo C., Raap J. (literal)
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- Institute of Chemical Kinetics and Combustion, Russian Academy of Science Novosibirsk, Russian Federation;
Institute of Mathematics, Russian Academy of Science Novosibirsk, Russian Federation;
Biopolymer Research Center, CNR, Department of Organic Chemistry, University of Padova, 35131 Padova, Italy;
Leiden Institute of Chemistry, Gorlaeus Laboratories, Leiden University, Leiden, The Netherlands (literal)
- Titolo
- Spatial distribution of spin-labeled trichogin GA IV in the Gram-positive bacterial cell membrane determined from PELDOR data (literal)
- Abstract
- Trichogin GA IV is one of the shortest acyclic linear polypeptide antibiotics of fungal origin, characterized by the presence of three alpha-amino isobutyric acid residues, an N-octanoyl group and an amino alcohol at the C terminus. Its antibiotic activity is generally thought to be based on its self-assembling and membrane-modifying properties. The technique of double electron-electron resonance in electron spin echo is used to study the spatial distribution of spin-labeled [TOAC-4]trichogin GA IV analog bound to the cell membrane of the Gram-positive bacterium Micrococcus luteus. The intermolecular dipole-dipole spin-spin interaction of TOAC spin labels has been experimentally studied at 77 K in glassy dispersions of the spherical cell particles. It is shown that the nonaggregated peptide molecules are distributed at the cytoplasmic membrane. Two possible distribution models are proposed: (i) the peptide molecules are randomly distributed on both inner and outer membrane surfaces with a distance between the surfaces of 7 run, (ii) the molecules are randomly distributed in a layer up to 2.4 mn from the external surface of the membrane. (literal)
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