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  • 1
    Publication Date: 2005-10-08
    Description: Most people hold beliefs about personality characteristics typical of members of their own and others' cultures. These perceptions of national character may be generalizations from personal experience, stereotypes with a "kernel of truth," or inaccurate stereotypes. We obtained national character ratings of 3989 people from 49 cultures and compared them with the average personality scores of culture members assessed by observer ratings and self-reports. National character ratings were reliable but did not converge with assessed traits. Perceptions of national character thus appear to be unfounded stereotypes that may serve the function of maintaining a national identity.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2775052/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2775052/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Terracciano, A -- Abdel-Khalek, A M -- Adam, N -- Adamovova, L -- Ahn, C-k -- Ahn, H-n -- Alansari, B M -- Alcalay, L -- Allik, J -- Angleitner, A -- Avia, M D -- Ayearst, L E -- Barbaranelli, C -- Beer, A -- Borg-Cunen, M A -- Bratko, D -- Brunner-Sciarra, M -- Budzinski, L -- Camart, N -- Dahourou, D -- De Fruyt, F -- de Lima, M P -- del Pilar, G E H -- Diener, E -- Falzon, R -- Fernando, K -- Fickova, E -- Fischer, R -- Flores-Mendoza, C -- Ghayur, M A -- Gulgoz, S -- Hagberg, B -- Halberstadt, J -- Halim, M S -- Hrebickova, M -- Humrichouse, J -- Jensen, H H -- Jocic, D D -- Jonsson, F H -- Khoury, B -- Klinkosz, W -- Knezevic, G -- Lauri, M A -- Leibovich, N -- Martin, T A -- Marusic, I -- Mastor, K A -- Matsumoto, D -- McRorie, M -- Meshcheriakov, B -- Mortensen, E L -- Munyae, M -- Nagy, J -- Nakazato, K -- Nansubuga, F -- Oishi, S -- Ojedokun, A O -- Ostendorf, F -- Paulhus, D L -- Pelevin, S -- Petot, J-M -- Podobnik, N -- Porrata, J L -- Pramila, V S -- Prentice, G -- Realo, A -- Reategui, N -- Rolland, J-P -- Rossier, J -- Ruch, W -- Rus, V S -- Sanchez-Bernardos, M L -- Schmidt, V -- Sciculna-Calleja, S -- Sekowski, A -- Shakespeare-Finch, J -- Shimonaka, Y -- Simonetti, F -- Sineshaw, T -- Siuta, J -- Smith, P B -- Trapnell, P D -- Trobst, K K -- Wang, L -- Yik, M -- Zupancic, A -- McCrae, R R -- Z99 AG999999/Intramural NIH HHS/ -- ZIA AG000180-25/Intramural NIH HHS/ -- ZIA AG000180-26/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2005 Oct 7;310(5745):96-100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institute on Aging, NIH, DHHS, Gerontology Research Center, 5600 Nathan Shock Drive, Baltimore, MD 21224, USA. terraccianoa@grc.nia.nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16210536" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; *Character ; Cross-Cultural Comparison ; *Culture ; *Ethnic Groups ; Female ; Humans ; Male ; *Personality ; Personality Assessment ; Reproducibility of Results ; Social Perception ; Stereotyping ; Surveys and Questionnaires
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Macromolecules 19 (1986), S. 2083-2085 
    ISSN: 1520-5835
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 94 (1991), S. 8210-8215 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: The solvent mediated force between the hard solutes mimicking liophobic colloids in Baxter's adhesive solvent is studied on the basis of the solution to the Percus–Yevick/Ornstein–Zernike equation for spatial correlations in an infinitely dilute solution. The contact value of the solute–solute potential of mean force remains the same as observed previously in hard sphere fluid but its range increases in the presence of the attractive interaction among the molecules of the solvent. At the critical conditions of the model fluid, the solvation force between the macroparticles tends to vanish in parallel with the increasing compressibility of the fluid. The size dependence of the intercolloidal interaction is similar but slightly more pronounced than found in fluids with pure hard core interaction.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 94 (1991), S. 586-589 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: The structure of the primitive model fused salt in planar slit is studied by Monte Carlo simulation. The density profile of the ionic melt in the slit with respect to the walls displays oscillations similar to those observed with simple liquids. At the pore width of about seven ionic diameters, the pressure exerted on the walls is comparable to the virial pressure of the bulk melt. The calculated surface energy of 210+20 mN m−1 is close to the experimental value for molten potassium chloride at similar conditions.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 89 (1988), S. 545-550 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: Thermodynamics of protein solubilization in water-in-oil microemulsions is analyzed in terms of the shell-and-core model for reverse micelles. The electrostatic contribution to the free energy of transfer of the protein from the aqueous solution to the microemulsion is determined via the solution of the nonlinear Poisson–Boltzmann equation for the protein/reverse micelle complex, for the protein-free micelle, and for the cell model of aqueous protein solution in equilibrium with the microemulsion. The electrolyte effect on the protein solubility in the microemulsion is studied. A good agreement between the predictions of the model and the known salting out effect of cytochrome-c in sodium di-2-ethylhexylsulfosuccinate AOT-water-in-isooctane microemulsion is observed.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 86 (1987), S. 2955-2959 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: The solvation force between neutral surfaces in water is studied by running the grand canonical ensemble Monte Carlo simulations on the system containing up to 102 water-like particles between parallel smooth plates immersed in the fluid. The water molecules are modeled like hard spheres with embedded point dipoles and orientation dependent adhesion potential. The pressure between the walls as a function of the distance displays oscillations resembling those observed experimentally, The overall attraction between the plates is observed despite the absence of direct wall–wall or wall–fluid attractive forces.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 92 (1990), S. 642-648 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: The electrostatic contribution to the interaction between reverse micelles in water-in-oil microemulsions formed in the presence of ionizing surfactant is studied by means of Monte Carlo simulation. The inverted micelles are treated as spherical entities consisting of charged surfactant shell and aqueous core with neutralizing counterions. The distributions of simple ions in the core determined by simulation are compared with the predictions of the Poisson–Boltzmann approximation. A good agreement is observed, particularly for monovalent simple ions. The dispersion force due to the correlated fluctuations in ionic distribution within electroneutral micelles is found to be of comparable magnitude as classical van der Waals interaction and may represent a significant contribution to the total pair potential estimated from recent small angle neutron scattering (SANS) measurements of intermicellar correlations.
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  • 8
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 92 (1990), S. 3741-3747 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: We present the analytic solution of the molecular Ornstein–Zernike equation for a very general closure in which the direct correlation function is of the form suggested by the mean-spherical approximation for arbitrary multipolar interactions and the total correlation function contains terms that arise in the Percus–Yevick approximation for spheres with anisotropic surface adhesion. In addition to generalizing several earlier analyses of special cases of this closure, the solution presented here contains new simplifying insights that reduce the complexity of the resulting algebraic equations. A special case of the analysis is described to illustrate the method of solution.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 90 (1989), S. 2752-2757 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: The structure of hard sphere fluid confined to cylindrical capillaries in equilibrium with the bulk fluid phase is considered. Simple analytical approaches are examined and compared with the results of simultaneous grand canonical ensemble Monte Carlo simulations. The validity of the limiting law according to which the fluid density in the capillary approaches its fugacity in vanishingly narrow pores is confirmed. The truncated graphical expansion around the exact narrow pore limit is found to represent a useful approximation for very narrow capillaries. In systems with the pore diameter exceeding a few diameters of the spheres and at the reduced bulk densities of the fluid ρbσ3≤0.6, the Percus–Yevick approximation provides a satisfactory description of the fluid distribution.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 114 (2001), S. 561-569 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: Aggregation of protein molecules resulting in the loss of biological activity and the formation of insoluble deposits represents a serious problem for the biotechnology and pharmaceutical industries and in medicine. Considerable experimental and theoretical efforts are being made in order to improve our understanding of, and ability to control, the process. In the present work, we describe a Monte Carlo study of a multichain system of coarse-grained model proteins akin to lattice models developed for simulations of protein folding. The model is designed to examine the competition between intramolecular interactions leading to the native protein structure, and intermolecular association, resulting in the formation of aggregates of misfolded chains. Interactions between the segments are described by a variation of the Go potential [N. Go and H. Abe, Biopolymers 20, 1013 (1981)] that extends the recognition between attracting types of segments to pairs on distinct chains. For the particular model we adopt, the global free energy minimum of a pair of protein molecules corresponds to a dimer of native proteins. When three or more molecules interact, clusters of misfolded chains can be more stable than aggregates of native folds. A considerable fraction of native structure, however, is preserved in these cases. Rates of conformational changes rapidly decrease with the size of the protein cluster. Within the timescale accessible to computer simulations, the folding-aggregation balance is strongly affected by kinetic considerations. Both the native form and aggregates can persist in metastable states, even if conditions such as temperature or concentration favor a transition to an alternative form. Refolding yield can be affected by the presence of an additional polymer species mimicking the function of a molecular chaperone. © 2001 American Institute of Physics.
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