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Showing 1 to 12 of 12 for “"Halobacterium halobium"”.

  1. Aerotaxis in HALOBACTERIUM HALOBIUM

    … was investigated in the archaebacterium <em>Halobacterium halobium.</em> A quantitative temporal assay for aerotaxis of <em>H. halobium</em> was developed using computer assisted motion analysis. Aerotaxis was most pronounced in early log phase cultures. Peak aerotaxis was found to coincide …

    loma-linda Repository record for Aerotaxis in HALOBACTERIUM HALOBIUM (opens in a new tab)

  2. Cation effects on the purple membrane of Halobacterium halobium

    My more recent research shows that the binding of one divalent cation is directly related to the blue-to-purple transition of bacteriorhodopsin; whereas, four other divalent cation binding sites involving carboxyl groups on the bacteriorhodopsin surface do not directly affect the color change. The …

    uiuc Repository record for Cation effects on the purple membrane of Halobacterium halobium (opens in a new tab)

  3. Thermodynamic and kinetic studies of purple membrane from halobacterium halobium

    … with the energy tranducing purple membrane from Halobacterium halobium. In the first experiment, we used flash photolysis to measure the effects of solvent viscosity on the kinetics of the purple membrane photocycle, and we analyzed the data in terms of a modified Kramers' theory. In the second …

    uiuc Repository record for Thermodynamic and kinetic studies of purple membrane from halobacterium halobium (opens in a new tab)

  4. Nuclear Magnetic Resonance Studies of Model and Biological Membranes

    … into the membrane protein, bacteriorhodopsin, of Halobacterium halobium. Our results indicate that there are at least two motional classes of amino acids in bacteriorhodopsin. The first type are rigid and give rise to the broad powder pattern observed. These amino acids are "matrix" amino acids …

    uiuc Repository record for Nuclear Magnetic Resonance Studies of Model and Biological Membranes (opens in a new tab)

  5. Isolation and characterization of new pterins from nonmethanogenic archaebacteria

    … One of these halopterins is produced by Halobacterium salinarium, Halobacterium halobium, and Halococcus morrhuae and is called phosphohalopterin-1. It was given this name because it was the first halopterin discovered and it has four monophosphate esters per dimeric pterin. The proposed …

    vt Repository record for Isolation and characterization of new pterins from nonmethanogenic archaebacteria (opens in a new tab)

  6. A Deuterium Nuclear Magnetic Resonance Study of Amino Acid Dynamics in the Membrane Protein, Bacteriorhodopsin (Nmr)

    … in the photosynthetic purple membrane of Halobacterium halobium. For L{(beta)-('2)H(,3)} alanine, DL{(gamma)-('2)H(,6)} valine, DL{(beta),(gamma)-('2)H(,4)} threonine, L{(delta)-('2)H(,3)} leucine, L{(alpha),(beta),(gamma),(gamma)',(delta)-('2)H(,10)} isoleucine, L{(epsilon)-('2)H(,3)} …

    uiuc Repository record for A Deuterium Nuclear Magnetic Resonance Study of Amino Acid Dynamics in the Membrane Protein, Bacteriorhodopsin (Nmr) (opens in a new tab)

  7. Molecular dynamics studies of the protein bacteriorhodopsin

    … residues in the purple membrane of the bacterium Halobacterium halobium. Bacteriorhodopsin undergoes a light-driven cyclic process, which pumps protons across the membrane, in order to maintain a proton gradient necessary for ATP synthesis. The cycle is initiated through a trans --+ cis …

    uiuc Repository record for Molecular dynamics studies of the protein bacteriorhodopsin (opens in a new tab)

  8. Molecular Dynamics and Quantum Chemistry Studies of the Protein Bacteriorhodopsin

    … residues in the purple membrane of the bacterium Halobacterium halobium. Bacteriorhodopsin undergoes a light-driven cyclic process, which pumps protons across the membrane, in order to maintain a proton gradient necessary for ATP synthesis. The cycle is initiated through a trans &rarr; cis …

    uiuc Repository record for Molecular Dynamics and Quantum Chemistry Studies of the Protein Bacteriorhodopsin (opens in a new tab)