Benzophenone photophore flexibility and proximity: Molecular and crystal-state structure of a Bpa-containing trichogin dodecapeptide analogue(487 views) Saviano M, Improta R, Benedetti E, Carrozzini B, Cascarano GL, Didierjean C, Toniolo C, Crisma M
Keywords: Conformation Analysis, Donor-Acceptor Systems, Helical Structures, Lipopeptaibol Antibiotic, X-Ray Diffraction, Benzophenone, Peptide Derivative, 4 Benzoylphenylalanine, 4-Benzoylphenylalanine, Antiinfective Agent, Benzophenone Derivative, Drug Derivative, Glycopeptide, Oligopeptide, Trichogin Ga Iv, Article, Chemical Structure, Crystal Structure, Hydrogen Bond, Molecular Interaction, Priority Journal, Protein Protein Interaction, X Ray Diffraction, Chemistry, Crystallization, Photochemistry, Pliability, X Ray Crystallography, Anti-Bacterial Agents, Hydrogen Bonding, Models, Molecular Structure,
Affiliations: *** IBB - CNR ***
Inst. of Biostructures/Bioimaging, CNR, via Mezzocannone 6, 80134 Napoli, Italy
Department of Biological Chemistry, Universita di Napoli Federico II, via Mezzocannone 6, 80134 Napoli, Italy
Institute of Crystallography, Department of Geomineralogy, University Campus, 70125 Bari, Italy
Groupe de Biocristallographie, Universite Henri Poincare Nancy I, Faculté des Sciences, B.P. 239, 54506 Vandoeuvre-les-Nancy Cedex, France
Institute of Biomolecular Chemistry, Department of Organic Chemistry, Università di Padova, via Marzolo 1, 35131 Padova, Italy
References: Not available.
Benzophenone photophore flexibility and proximity: Molecular and crystal-state structure of a Bpa-containing trichogin dodecapeptide analogue
Up close and flexible: An X-ray diffraction analysis of a Bpa-containing analogue of the lipopeptaibol trichogin GA IV strongly points to the conclusion that caution should be exercised in utilizing this highly flexible, benzophenone-based photoprobe acritically in biochemical and biophysical studies. As a result of the different side-chain conformations adopted by the Bpa residue, the distance of its ketone carbonyl carbon from the midpoint of the N-O bond of the nitroxide-containing side chain of the TOAC residue in the two crystallographically independent peptide molecules differs by as much as 11 Å as shown in the figure.
Benzophenone photophore flexibility and proximity: Molecular and crystal-state structure of a Bpa-containing trichogin dodecapeptide analogue
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Benzophenone photophore flexibility and proximity: Molecular and crystal-state structure of a Bpa-containing trichogin dodecapeptide analogue