Inside Cover: Stability and Shape of Hepatitis B Virus Capsids In Vacuo (Angew. Chem. Int. Ed. 33/2008)

Authors

  • Charlotte Uetrecht,

    1. Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht (The Netherlands), Fax: (+31) 30-251-8219
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  • Cees Versluis,

    1. Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht (The Netherlands), Fax: (+31) 30-251-8219
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  • Norman R. Watts,

    1. Protein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892 (USA)
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  • Paul T. Wingfield,

    1. Protein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892 (USA)
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  • Alasdair C. Steven,

    1. Laboratory of Structural Biology Research, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892 (USA)
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  • Albert J. R. Heck Prof. Dr.

    1. Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht (The Netherlands), Fax: (+31) 30-251-8219
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Abstract

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Precise biophysical characterization of macromolecular complexes is possible by mass spectrometry. Heck et al. report in their Communication on page 6247 ff. how two distinct icosahedral geometries of intact megaDalton capsids of the hepatitis B virus (a major human pathogen) can be measured and separated by mass spectrometry. Ion mobility measurements established that the viral structures are largely preserved in vacuo and two distinct conformers per capsid geometry could be distinguished.

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