54 research outputs found
Flat extensions of positive moment matrices: recursively generated relations
We develop new computational tests for existence and uniqueness of representing measures in the Truncated Complex Moment Problem: Îłij = Z zizj d (0 i + j 2n):(TCMP) We characterize the existence of nitely atomic representing measures in terms of positivity and extension properties of the moment matrix M(n)(Îł) associated with Îł Îł(2n): Îł00; : : : ; Îł0;2n; : : : ; Îł2n;0, Îł00> 0 (Theorem 1.5). We study conditions for flat (i.e., rank-preserving) extensions M(n + 1) of M(n) 0; each such extension corresponds to a distinct rank M(n)-atomic representing measure, and each such measure is minimal among representing measures in terms of the cardinality of its support. For a natural class of moment matrices satisfying the tests of recursive generation, recursive consis-tency, and normal consistency, we reduce the existence problem for minimal representing measures to the solubility of small systems of multivariable alge
n-Tuples of operators satisfying ÏT(AB)=ÏT(BA)
AbstractFor âcriss-cross commutingâ tuples A and B of Banach space operators we give two sufficient conditions for the spectral equality ÏT(AB)=ÏT(BA)
Subnormality for arbitrary powers of 2-variable weighted shifts whose restrictions to a large invariant subspace are tensor products
The Lifting Problem for Commuting Subnormals (LPCS) asks for necessary and
sufficient conditions for a pair of subnormal operators on Hilbert space to
admit commuting normal extensions. \ We study LPCS within the class of
commuting 2-variable weighted shifts with
subnormal components and , acting on the Hilbert space with canonical orthonormal basis
. \ The \textit{core} of a commuting
2-variable weighted shift , , is the restriction of
to the invariant subspace generated by all vectors
with ; we say that is of \textit{tensor form}
if it is unitarily equivalent to a shift of the form , where and are subnormal unilateral
weighted shifts. \ Given a 2-variable weighted shift whose core is
of tensor form, we prove that LPCS is solvable for if and only if
LPCS is solvable for any power (). \Comment: article in pres
Toral and spherical Aluthge transforms of 2-variable weighted shifts
We introduce two natural notions of Aluthge transforms (toral and spherical)
for 2-variable weighted shifts and study their basic properties. Next, we study
the class of spherically quasinormal -variable weighted shifts, which are
the fixed points for the spherical Aluthge transform. Finally, we briefly
discuss the relation between spherically quasinormal and spherically isometric
2-variable weighted shifts.Comment: Accepted for publication by C.R. Acad. Sci. Paris, Ser. I (2016
Time-dependent moments from partial differential equations and the time-dependent set of atoms
We study the time-dependent moments of the solution of the partial differential equation
with initial Schwartz
function data . At first we describe the dual
action on the polynomials, i.e., the time-evolution of is completely moved
to the polynomial side . We
investigate the special case of the heat equation. We find that several
non-negative polynomials which are not sums of squares become sums of squares
under the heat equation in finite time. Finally, we solve the problem of moving
atoms under the equation with being a finitely atomic measure. We find that in the time evolution
the atom positions
are governed only by the transport term and that the
time-dependent coefficients have an analytic solution depending on
Subnormality of Bergman-like weighted shifts
Abstract For a, b, c, d 0 with ad â bc > 0, we consider the unilateral weighted shift S (a, b, c, d) with weights α n := an+b cn+d (n 0). Using Schur product techniques, we prove that S (a, b, c, d) is always subnormal; more generally, we establish that for every p 1, all p-subshifts of S (a, b, c, d
N-terminal mutants of human apolipoprotein A-I : Structural perturbations associated to protein misfolding
Since the early description of different human apolipoprotein A-I variants associated to amyloidosis, the reason that determines its deposition inducing organ failure has been under research. To shed light into the events associated to protein aggregation, we studied the effect of the structural perturbations induced by the replacement of a Leucine in position 60 by an Arginine as it occurs in the natural amyloidogenic variant (L60R). Circular dichroism, intrinsic fluorescence measurements and assays of binding to ligands indicate that L60R is more unstable, more sensitive to proteolysis and interacts with sodium dodecyl sulfate (a model of negative lipids) more than the protein with the native sequence and other natural variant tested, involving a replacement of a Trytophan by and Arginine in the amino acid 50 (W50R). In addition, the small structural rearrangement observed under physiological pH leads to the release of tumor necrosis factor α and interleukin-lÎČ from a model of macrophages. Our results strongly suggest that the chronic disease may be a consequence of the loss in the native conformation which alters the equilibrium among native and cytotoxic proteins conformation.Instituto de Investigaciones BioquĂmicas de La PlataFacultad de Ciencias MĂ©dicasInstituto de Investigaciones FisicoquĂmicas TeĂłricas y Aplicada
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