| Literature DB >> 20858439 |
Astrid C Sivertsen1, Marvin J Bayro, Marina Belenky, Robert G Griffin, Judith Herzfeld.
Abstract
Gas vesicles are gas-filled buoyancy organelles with walls that consist almost exclusively of gas vesicle protein A (GvpA). Intact, collapsed gas vesicles from the cyanobacterium Anabaena flos-aquae were studied by solid-state NMR spectroscopy, and most of the GvpA sequence was assigned. Chemical shift analysis indicates a coil-α-β-β-α-coil peptide backbone, consistent with secondary-structure-prediction algorithms, and complementary information about mobility and solvent exposure yields a picture of the overall topology of the vesicle subunit that is consistent with its role in stabilizing an air-water interface.Entities:
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Year: 2010 PMID: 20858439 PMCID: PMC2941023 DOI: 10.1016/j.bpj.2010.06.041
Source DB: PubMed Journal: Biophys J ISSN: 0006-3495 Impact factor: 4.033