95,199 research outputs found

    Conditions for Nondistortion Interrogation of Quantum System

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    Under some physical considerations, we present a universal formulation to study the possibility of localizing a quantum object in a given region without disturbing its unknown internal state. When the interaction between the object and probe wave function takes place only once, we prove the necessary and sufficient condition that the object's presence can be detected in an initial state preserving way. Meanwhile, a conditioned optimal interrogation probability is obtained.Comment: 5 pages, Revtex, 1 figures, Presentation improved, corollary 1 added. To appear in Europhysics Letter

    The demagnetization factor for randomly packed spheroidal particles

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    We investigate if the demagnetization factor for a randomly packed powder of magnetic spheroidal particles depend on the shape of the spheroidal particles and what the internal variation in magnetization is within such a powder. A spheroid is an ellipsoid of revolution, i.e. an ellipsoid with two semi-major axis being equal. The demagnetization factor is calculated as function of particle aspect ratio using two independent numerical models for several different packings, and assuming a relative permeability of 2. The calculated demagnetization factor is shown to depend on particle aspect ratio, not because of direct magnetic interaction but because the particle packing depend on the aspect ratio of the particles. The relative standard deviation of the magnetization across the powder was 3\%-8\%, increasing as the particle shape deviates from spherical, while the relative standard deviation within each particle was relatively constant around 5\%.Comment: 7 pages, 9 figure

    Protein chainmail variants in dsDNA viruses.

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    First discovered in bacteriophage HK97, biological chainmail is a highly stable system formed by concatenated protein rings. Each subunit of the ring contains the HK97-like fold, which is characterized by its submarine-like shape with a 5-stranded β sheet in the axial (A) domain, spine helix in the peripheral (P) domain, and an extended (E) loop. HK97 capsid consists of covalently-linked copies of just one HK97-like fold protein and represents the most effective strategy to form highly stable chainmail needed for dsDNA genome encapsidation. Recently, near-atomic resolution structures enabled by cryo electron microscopy (cryoEM) have revealed a range of other, more complex variants of this strategy for constructing dsDNA viruses. The first strategy, exemplified by P22-like phages, is the attachment of an insertional (I) domain to the core 5-stranded β sheet of the HK97-like fold. The atomic models of the Bordetella phage BPP-1 showcases an alternative topology of the classic HK97 topology of the HK97-like fold, as well as the second strategy for constructing stable capsids, where an auxiliary jellyroll protein dimer serves to cement the non-covalent chainmail formed by capsid protein subunits. The third strategy, found in lambda-like phages, uses auxiliary protein trimers to stabilize the underlying non-covalent chainmail near the 3-fold axis. Herpesviruses represent highly complex viruses that use a combination of these strategies, resulting in four-level hierarchical organization including a non-covalent chainmail formed by the HK97-like fold domain found in the floor region. A thorough understanding of these structures should help unlock the enigma of the emergence and evolution of dsDNA viruses and inform bioengineering efforts based on these viruses
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