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  • 1
    Publication Date: 2008-12-19
    Description: Geometric frustration arises when lattice structure prevents simultaneous minimization of local interaction energies. It leads to highly degenerate ground states and, subsequently, to complex phases of matter, such as water ice, spin ice, and frustrated magnetic materials. Here we report a simple geometrically frustrated system composed of closely packed colloidal spheres confined between parallel walls. Diameter-tunable microgel spheres are self-assembled into a buckled triangular lattice with either up or down displacements, analogous to an antiferromagnetic Ising model on a triangular lattice. Experiment and theory reveal single-particle dynamics governed by in-plane lattice distortions that partially relieve frustration and produce ground states with zigzagging stripes and subextensive entropy, rather than the more random configurations and extensive entropy of the antiferromagnetic Ising model. This tunable soft-matter system provides a means to directly visualize the dynamics of frustration, thermal excitations and defects.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Han, Yilong -- Shokef, Yair -- Alsayed, Ahmed M -- Yunker, Peter -- Lubensky, Tom C -- Yodh, Arjun G -- England -- Nature. 2008 Dec 18;456(7224):898-903. doi: 10.1038/nature07595.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics and Astronomy, University of Pennsylvania, 209 South 33rd Street, Philadelphia, Pennsylvania 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19092926" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 2009-05-16
    Description: When the packing fraction is increased sufficiently, loose particulates jam to form a rigid solid in which the constituents are no longer free to move. In typical granular materials and foams, the thermal energy is too small to produce structural rearrangements. In this zero-temperature (T = 0) limit, multiple diverging and vanishing length scales characterize the approach to a sharp jamming transition. However, because thermal motion becomes relevant when the particles are small enough, it is imperative to understand how these length scales evolve as the temperature is increased. Here we used both colloidal experiments and computer simulations to progress beyond the zero-temperature limit to track one of the key parameters-the overlap distance between neighbouring particles-which vanishes at the T = 0 jamming transition. We find that this structural feature retains a vestige of its T = 0 behaviour and evolves in an unusual manner, which has masked its appearance until now. It is evident as a function of packing fraction at fixed temperature, but not as a function of temperature at fixed packing fraction or pressure. Our results conclusively demonstrate that length scales associated with the T = 0 jamming transition persist in thermal systems, not only in simulations but also in laboratory experiments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Zexin -- Xu, Ning -- Chen, Daniel T N -- Yunker, Peter -- Alsayed, Ahmed M -- Aptowicz, Kevin B -- Habdas, Piotr -- Liu, Andrea J -- Nagel, Sidney R -- Yodh, Arjun G -- England -- Nature. 2009 May 14;459(7244):230-3. doi: 10.1038/nature07998.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics and Astronomy, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA. zexin@sas.upenn.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19444211" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 2016-01-21
    Description: Single-span membrane proteins (ssMPs) represent approximately one-half of all membrane proteins and play important roles in cellular communications. However, like all membrane proteins, ssMPs are prone to misfolding and aggregation because of the hydrophobicity of transmembrane helices, making them difficult to study using common aqueous solution-based approaches. Detergents and membrane...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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