788 research outputs found
Simulation study of pressure and temperature dependence of the negative thermal expansion in Zn(CN)(2)
12 pages, 16 figures12 pages, 16 figures12 pages, 16 figures12 pages, 16 figure
Free-Field Realization of D-dimensional Cylindrical Gravitational Waves
We find two-dimensional free-field variables for D-dimensional general
relativity on spacetimes with D-2 commuting spacelike Killing vector fields and
non-compact spatial sections for D>4. We show that there is a canonical
transformation which maps the corresponding two-dimensional dilaton gravity
theory into a two-dimensional diffeomorphism invariant theory of the free-field
variables. We also show that the spacetime metric components can be expressed
as asymptotic series in negative powers of the dilaton, with coefficients which
can be determined in terms of the free fields.Comment: 15 pages, Late
Backreaction from non-conformal quantum fields in de Sitter spacetime
We study the backreaction on the mean field geometry due to a non-conformal
quantum field in a Robertson-Walker background. In the regime of small mass and
small deviation from conformal coupling, we compute perturbatively the
expectation value of the stress tensor of the field for a variety of vacuum
states, and use it to obtain explicitly the semiclassical gravity solutions for
isotropic perturbations around de Sitter spacetime, which is found to be
stable. Our results show clearly the crucial role of the non-local terms that
appear in the effective action: they cancel the contribution from local terms
proportional to the logarithm of the scale factor which would otherwise become
dominant at late times and prevent the existence of a stable self-consistent de
Sitter solution. Finally, the opposite regime of a strongly non-conformal field
with a large mass is also considered.Comment: 31 page
Stability of de Sitter spacetime under isotropic perturbations in semiclassical gravity
A spatially flat Robertson-Walker spacetime driven by a cosmological constant
is non-conformally coupled to a massless scalar field. The equations of
semiclassical gravity are explicitly solved for this case, and a
self-consistent de Sitter solution associated with the Bunch-Davies vacuum
state is found (the effect of the quantum field is to shift slightly the
effective cosmological constant). Furthermore, it is shown that the corrected
de Sitter spacetime is stable under spatially-isotropic perturbations of the
metric and the quantum state. These results are independent of the free
renormalization parameters.Comment: 19 pages, REVTeX
A multiply substituted G-H loop from foot-and-mouth disease virus in complex with a neutralizing antibody: A role for water molecules
The crystal structure of a 15 amino acid synthetic peptide, corresponding to the sequence of the major antigenic site A (G-H loop of VP1) from a multiple variant of foot-and-mouth disease virus (FMDV), has been determined at 2·3 resolution. The variant peptide includes four amino acid substitutions in the loop relative to the previously studied peptide representing FMDV C-S8c1 and corresponds to the loop of a natural FMDV isolate of subtype C1. The peptide was complexed with the Fab fragment of the neutralizing monoclonal antibody 4C4. The peptide adopts a compact fold with a nearly cyclic conformation and a disposition of the receptor-recognition motif Arg-Gly-Asp that is closely related to the previously determined structure for the viral loop, as part of the virion, and for unsubstituted synthetic peptide antigen bound to neutralizing antibodies. New structural findings include the observation that well-defined solvent molecules appear to play a major role in stabilizing the conformation of the peptide and its interactions with the antibody. Structural results are supported by molecular-dynamic simulations. The multiply substituted peptide developed compensatory mechanisms to bind the antibody with a conformation very similar to that of its unsubstituted counterpart. One water molecule, which for steric reasons could not occupy the same position in the unsubstituted antigen, establishes hydrogen bonds with three peptide amino acids. The constancy of the structure of an antigenic domain despite multiple amino acid substitutions has implications for vaccine design
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