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  • 1
    Electronic Resource
    Electronic Resource
    Profile unbiased thermostat with dynamical streaming velocities (1996)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 105 (1996), S. 11183-11189 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: We have devised a reversible set of nonequilibrium molecular dynamics equations of motion to study viscous flow under an applied shear field utilizing a new profile unbiased thermostat (PUT). Based on a modification of the original equations presented by Evans and Morriss [Phys. Rev. Lett. 56, 2172 (1986)], we have extended the phase space to include dynamically evolving streaming velocities. The new method is advantageous because it allows control of the rate at which the streaming velocities evolve and thereby removes the effects of high frequency thermal fluctuations. Further, in tests on a Weeks–Chandler–Andersen fluid, we find that a shear-induced microstructure, the so-called "string phase,'' was not destabilized by the new PUT scheme. © 1996 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.472917
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  • 2
    Electronic Resource
    Electronic Resource
    The effects of pressure on structural and dynamical properties of associated liquids: Molecular dynamics calculations for the extended simple point charge model of water (1997)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 107 (1997), S. 8561-8567 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: Constant temperature and constant pressure molecular dynamics calculations have been performed on the extended simple point charge (SPC/E) model water to understand the effects of pressure on its structural and dynamical properties. The effect of pressure is to increase the presence of interstitial water molecules, which is shown to be responsible for the experimentally observed increase in the first x-ray diffraction peak and a broadening of the OOO&dbgcaret; bond angle distribution. These structural changes lead to weaker hydrogen bonding and the observed minimum in the rotational correlation time as a function of pressure. The weak maximum in the measured translational diffusion coefficient at around 1.5 kbar was not reproduced. The temperature of the density maximum was estimated to occur at 245±4 K, which suggests that structural changes with increasing pressure and decreasing temperature are not quantitatively reproduced by the SPC/E model. © 1997 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.475162
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  • 3
    Electronic Resource
    Electronic Resource
    Conformational preferences of oligopeptides rich in α-aminoisobutyric acid. I. Observation of a 310/α-helical transition upon sequence permutation (1991)
    New York : Wiley-Blackwell
    Biopolymers 31 (1991), S. 1763-1774 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The solution conformation of peptides rich in the α,α-dialkylated amino acid Aib has proven to be a subtle problem, not because of helix/coil transitions, but rather because of α-helical/310-helical competition. A special series of peptides containing 75% Aib has been synthesized that feature identical amino acid composition but differing sequences; they are sequence permutation isomers. Nuclear magnetic resonance hydrogen-bonding studies reveal that there is a sequence permutation induced transition between the two alternative helical forms within this set. The implications for the design and conformational prediction of helical Aib-rich peptides are discussed.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360311410
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