title: Solid-state NMR characterization of gas vesicle structure.
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.
authors.affiliation: Department of Chemistry, Brandeis University, Waltham, Massachusetts, USA.
authors.forename: Astrid C
authors.initials: AC
authors.lastname: Sivertsen
authors.forename: Marvin J
authors.initials: MJ
authors.lastname: Bayro
authors.forename: Marina
authors.initials: M
authors.lastname: Belenky
authors.forename: Robert G
authors.initials: RG
authors.lastname: Griffin
authors.forename: Judith
authors.initials: J
authors.lastname: Herzfeld
mesh_terms: D017033:Anabaena; D005740:Gases; D057927:Hydrophobic and Hydrophilic Interactions; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D009068:Movement; D015388:Organelles / Q000737:chemistry*; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry / Q000378:metabolism; D012997:Solvents / Q000737:chemistry
chemical_list: D005740:Gases; D011506:Proteins; D012997:Solvents; C038524:gas vesicle protein