Author(s): Philip G. Judge, Alexandra Tritschler, Han Uitenbroek, Kevin Reardon, Gianna Cauzzi, and Alfred de Wijn
Affiliation(s): High Altitude Observatory, National Center for Atmospheric Research, P.O. Box 3000, Boulder, CO 80307-3000, USA; National Solar Observatory/Sacramento Peak, P.O. Box 62, Sunspot, NM 88349, USA; INAF–Ossevatorio Astrofisico di Arcetri, I-50125 Firenze, [...]
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Author(s): Carolus J. Schrijver Author(s): Eric E. Mamajek, Matthew A. Kenworthy, Philip M. Hinz, and Michael R. Meyer Author(s): Chris J. Willott, Philippe Delorme, Celine Reyle, Loic Albert, Jacqueline Bergeron, David Crampton, Xavier Delfosse, Thierry Forveille, John B. Hutchings, Ross J. McLure, Alain Omont, and David Schade Author(s): Matthew M. Knight, Michael F. A’Hearn, Douglas A. Biesecker, Guillaume Faury, Douglas P. Hamilton, Philippe Lamy, and Antoine Llebaria Author(s): Jae Woo Lee, Jae-Hyuck Youn, Wonyong Han, Chung-Uk Lee, Seung-Lee Kim, Ho-Il Kim, Jang-Ho Park, and Robert H. Koch Nitronyl nitroxide radicals linked with naphyridine carbamate dimer are noncovalently assembled into DNA duplexes containing a CGG/CGG triad as an addressable position, leading to the remarkable changes of line shapes in ESR [...] Publication year: 2010 Studies on the structural stability of rabbit prion probed by molecular dynamics simulations of its wild-type and mutants. J Theor Biol. 2010 Jan 25; Authors: Zhang J Prion diseases are invariably fatal and highly infectious neurodegenerative diseases that affect humans and animals. Rabbits are the only mammalian species reported to be resistant to infection from prion diseases isolated from other species (Vorberg I., H. G. Martin, P. Eberhard, and A. P. Suzette. 2003. Journal of Virology 77 (3): 2003-2009). Fortunately, the NMR structure of rabbit prion (124-228) (PDB entry 2FJ3), the NMR structure of rabbit prion protein mutation S173N (PDB entry 2JOH) and the NMR structure of rabbit prion protein mutation I214V (PDB entry 2JOM) were released recently. This paper studies these NMR structures by molecular dynamics simulations. Simulation results confirm the structural stability of wild-type rabbit prion, and show that the salt bridge between D177 and R163 greatly contributes to the structural stability of rabbit prion protein. PMID: 20109469 [PubMed - as supplied by publisher] [...] A solution to the accelerated-predator-satiety lotka-volterra predator-prey problem using boubaker polynomial expansion scheme. J Theor Biol. 2010 Jan 25; Authors: Dubey B, Zhao TG, Jonsson M, Rahmanov H In this study, an analytical method is introduced for the identification of predator-prey populations time-dependent evolution in a Lotka-Volterra predator-prey model which takes into account the concept of accelerated-predator-satiety. Oppositely to most of the predator-prey problem models, the actual model does not suppose that the predation is strictly proportional to the prey density. In reference to some recent experimental results and particularly to the conclusions of May (1973) about predators which are ‘never not hungry’, an accelerated satiety function is matched with the initial conventional equations. Solutions are plotted and compared to some relevant ones. The obtained trends are in good agreement with many standard Lotka-Volterra solutions except for the asymptotic behaviour. PMID: 20109470 [PubMed - as supplied by publisher] [...] |
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