1,846 research outputs found

    Symmetry breaking in crossed magnetic and electric fields

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    We present the first observations of cylindrical symmetry breaking in highly excited diamagnetic hydrogen with a small crossed electric field, and we give a semiclassical interpretation of this effect. As the small perpendicular electric field is added, the recurrence strengths of closed orbits decrease smoothly to a minimum, and revive again. This phenomenon, caused by interference among the electron waves that return to the nucleus, can be computed from the azimuthal dependence of the classical closed orbits.Comment: 4 page REVTeX file including 5 postscript files (using psfig) Accepted for publication in Physical Review Letters. Difference from earlier preprint: we have discovered the cause of the earlier apparent discrepancy between experiment and theory and now achieve excellent agreemen

    Context-dependent nature of destabilizing mutations on the stability of fkbp12

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    ABSTRACT: The context-dependent nature in which mutations affect protein stability was investigated using the FK506-binding protein, FKBP12. Thirty-four mutations were made at sites throughout the protein, including residues located in the hydrophobic core, the -sheet, and the solvent-exposed face of the R-helix. Urea-induced denaturation experiments were used to measure the change in stability of the mutants relative to that of the wild type (∆∆G U-F ). The results clearly show that the extent of destabilization, or stabilization, is highly context-dependent. Correlations were sought in order to link ∆∆G U-F to various structural parameters. The strongest correlation found was between ∆∆G U-F and N, the number of methyl-(ene) groups within a 6 Å radius of the group(s) deleted. For mutations of buried hydrophobic residues, a correlation coefficient of 0.73 (n ) 16,where n is the number of points) was obtained. This increased to 0.81 (n ) 24) on inclusion of mutations of partially buried hydrophobic residues. These data could be superimposed on data obtained for other proteins for which similarly detailed studies have been performed. Thus, the contribution to stability from hydrophobic side chains, independent of the extent to which a side chain is buried, can be estimated quantitatively using N. This correlation appears to be a general feature of all globular proteins. The effect on stability of mutating polar and charged residues in the R-helix and -sheet was also found to be highly context-dependent. Previous experimental and statistical studies have shown that specific side chains can stabilize the N-caps of R-helices in proteins. Substitutions of Ile56 to Thr and Asp at the N-cap of the R-helix of FKBP12, however, were found to be highly destabilizing. Thus, the intrinsic propensities of an amino acid for a particular element of secondary structure can easily be outweighed by tertiary packing factors. This study highlights the importance of packing density in determining the contribution of a residue to protein stability. This is the most important factor that should be taken into consideration in protein design. To design novel proteins, or rationally alter existing ones, a quantitative understanding of the factors that affect the stability of the native state is required. For proteins without disulfide bonds, noncovalent interactionsssuch as hydrophobic interactions, hydrogen bonds, and electrostatic interactionssdetermine protein stability (1). Protein engineering studies have provided an abundance of information on the relationship between protein structure and stability. Studies on hydrophobic groups (2-13) have shown that the packing of nonpolar groups and burial of hydrophobic surface area are the dominant forces in the stabilization of proteins. Studies on both fully and partially buried hydrophobic residues in barnase, CI2, and staphylococcal nuclease have shown correlations between the change in protein stability upon mutation (∆∆G U-F ) and both the packing density [number of methyl(ene) groups within a certain radius of the nonpolar groups removed

    Setting up tunneling conditions by means of Bohmian mechanics

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    Usually tunneling is established after imposing some matching conditions on the (time-independent) wave function and its first derivative at the boundaries of a barrier. Here an alternative scheme is proposed to determine tunneling and estimate transmission probabilities in time-dependent problems, which takes advantage of the trajectory picture provided by Bohmian mechanics. From this theory a general functional expression for the transmission probability in terms of the system initial state can be reached. This expression is used here to analyze tunneling properties and estimate transmissions in the case of initial Gaussian wave packets colliding with ramp-like barriers.Comment: 18 pages, 4 figure

    Power Laws, Precursors and Predictability During Failure

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    We investigate the dynamics of a modified Burridge-Knopoff model by introducing a dissipative term to mimic the bursts of acoustic emission (AE) from rock samples. The model explains many features of the statistics of AE signals observed in experiments such as the crossover in the exponent value from relatively small amplitude AE signals to larger regime, and their dependence on the pulling speed. Significantly, we find that the cumulative energy dissipated identified with acoustic emission can be used to predict a major slip event. We also find a data collapse of the acoustic activity for several major slip events describable by a universal stretched exponential with corrections in terms of time-to-failure.Comment: 7 pages, 6 figures, Final version with minor change
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