358 research outputs found
Statistical properties of contact vectors
We study the statistical properties of contact vectors, a construct to
characterize a protein's structure. The contact vector of an N-residue protein
is a list of N integers n_i, representing the number of residues in contact
with residue i. We study analytically (at mean-field level) and numerically the
amount of structural information contained in a contact vector. Analytical
calculations reveal that a large variance in the contact numbers reduces the
degeneracy of the mapping between contact vectors and structures. Exact
enumeration for lengths up to N=16 on the three dimensional cubic lattice
indicates that the growth rate of number of contact vectors as a function of N
is only 3% less than that for contact maps. In particular, for compact
structures we present numerical evidence that, practically, each contact vector
corresponds to only a handful of structures. We discuss how this information
can be used for better structure prediction.Comment: 20 pages, 6 figure
Produtividade e características agronômicas de Brachiaria brizantha cv. Paiaguás submetida a doses de nitrogênio sob cortes
Objetivou-se descrever a resposta da Brachiaria brizantha cv. Paiaguás em doses de adubação nitrogenada no segundo ano de produção. O experimento foi conduzido na área experimental da Universidade do Estado de Mato Grosso, localizada no município de Tangará da Serra, em blocos casualizados, com seis tratamentos (doses de 0, 50, 100, 150, 200 e 250 kg/ha de N) e quatro repetições, em parcelas de 9 m2 cada. As doses foram parceladas em quatro vezes, aplicadas após cada corte. Observou-se efeito significativo (P ≤ 0,05) para as variáveis alturas de plantas, número de perfilhos/m2, porcentagem de matéria seca, massa verde/ha, massa seca/ha, massa seca de folhas e massa seca de colmos/ha. Os resultados mostram que em doses de 250 kg/ha de N, com condições climáticas favoráveis ao crescimento da forragem há efeito positivo do N sobre o número de perfilhos/m2, a massa seca/ha, a massa seca de folhas e a massa seca de colmos/ha de Brachiaria brizantha cv. Paiaguás
On the form of growing strings
Patterns and forms adopted by Nature, such as the shape of living cells, the
geometry of shells and the branched structure of plants, are often the result
of simple dynamical paradigms. Here we show that a growing self-interacting
string attached to a tracking origin, modeled to resemble nascent polypeptides
in vivo, develops helical structures which are more pronounced at the growing
end. We also show that the dynamic growth ensemble shares several features of
an equilibrium ensemble in which the growing end of the polymer is under an
effective stretching force. A statistical analysis of native states of proteins
shows that the signature of this non-equilibrium phenomenon has been fixed by
evolution at the C-terminus, the growing end of a nascent protein. These
findings suggest that a generic non-equilibrium growth process might have
provided an additional evolutionary advantage for nascent proteins by favoring
the preferential selection of helical structures.Comment: 4 pages, 3 figures. Accepted for publication in Phys. Rev. Let
Proteome-wide observation of the phenomenon of life on the edge of solubility
To function effectively proteins must avoid aberrant aggregation, and hence they are expected to be expressed at concentrations safely below their solubility limits. By analyzing proteome-wide mass spectrometry data of Caenorhabditis elegans, however, we show that the levels of about three-quarters of the nearly 4, 000 proteins analyzed in adult animals are close to their intrinsic solubility limits, indeed exceeding them by about 10% on average. We next asked how aging and functional self-assembly influence these solubility limits. We found that despite the fact that the total quantity of proteins within the cellular environment remains approximately constant during aging, protein aggregation sharply increases between days 6 and 12 of adulthood, after the worms have reproduced, as individual proteins lose their stoichiometric balances and the cellular machinery that maintains solubility undergoes functional decline. These findings reveal that these proteins are highly prone to undergoing concentration-dependent phase separation, which on aging is rationalized in a decrease of their effective solubilities, in particular for proteins associated with translation, growth, reproduction, and the chaperone system
Dynamical chaos and power spectra in toy models of heteropolymers and proteins
The dynamical chaos in Lennard-Jones toy models of heteropolymers is studied
by molecular dynamics simulations. It is shown that two nearby trajectories
quickly diverge from each other if the heteropolymer corresponds to a random
sequence. For good folders, on the other hand, two nearby trajectories may
initially move apart but eventually they come together. Thus good folders are
intrinsically non-chaotic. A choice of a distance of the initial conformation
from the native state affects the way in which a separation between the twin
trajectories behaves in time. This observation allows one to determine the size
of a folding funnel in good folders. We study the energy landscapes of the toy
models by determining the power spectra and fractal characteristics of the
dependence of the potential energy on time. For good folders, folding and
unfolding trajectories have distinctly different correlated behaviors at low
frequencies.Comment: 8 pages, 9 EPS figures, Phys. Rev. E (in press
Critical exponents of the anisotropic Bak-Sneppen model
We analyze the behavior of spatially anisotropic Bak-Sneppen model. We
demonstrate that a nontrivial relation between critical exponents tau and
mu=d/D, recently derived for the isotropic Bak-Sneppen model, holds for its
anisotropic version as well. For one-dimensional anisotropic Bak-Sneppen model
we derive a novel exact equation for the distribution of avalanche spatial
sizes, and extract the value gamma=2 for one of the critical exponents of the
model. Other critical exponents are then determined from previously known
exponent relations. Our results are in excellent agreement with Monte Carlo
simulations of the model as well as with direct numerical integration of the
new equation.Comment: 8 pages, three figures included with psfig, some rewriting, + extra
figure and table of exponent
Critical Casimir effect in films for generic non-symmetry-breaking boundary conditions
Systems described by an O(n) symmetrical Hamiltonian are considered
in a -dimensional film geometry at their bulk critical points. A detailed
renormalization-group (RG) study of the critical Casimir forces induced between
the film's boundary planes by thermal fluctuations is presented for the case
where the O(n) symmetry remains unbroken by the surfaces. The boundary planes
are assumed to cause short-ranged disturbances of the interactions that can be
modelled by standard surface contributions corresponding
to subcritical or critical enhancement of the surface interactions. This
translates into mesoscopic boundary conditions of the generic
symmetry-preserving Robin type .
RG-improved perturbation theory and Abel-Plana techniques are used to compute
the -dependent part of the reduced excess free energy per
film area to two-loop order. When , it takes the scaling
form as
, where are scaling fields associated with the
surface-enhancement variables , while is a standard
surface crossover exponent. The scaling function
and its analogue for the Casimir force
are determined via expansion in and extrapolated to
dimensions. In the special case , the expansion
becomes fractional. Consistency with the known fractional expansions of D(0,0)
and to order is achieved by appropriate
reorganisation of RG-improved perturbation theory. For appropriate choices of
and , the Casimir forces can have either sign. Furthermore,
crossovers from attraction to repulsion and vice versa may occur as
increases.Comment: Latex source file, 40 pages, 9 figure
Infestação por ictio em surubim híbrido durante a fase inicial de criação.
bitstream/item/42263/1/COT-165-2011.pd
Intrinsic determinants of neurotoxic aggregate formation by the amyloid β peptide
The extent to which proteins aggregate into distinct structures ranging from prefibrillar oligomers to amyloid fibrils is key to the pathogenesis of many age-related degenerative diseases. We describe here for the Alzheimer's disease-related amyloid β peptide (Aβ) an investigation of the sequence-based determinants of the balance between the formation of prefibrillar aggregates and amyloid fibrils. We show that by introducing single-point mutations, it is possible to convert the normally harmless Aβ40 peptide into a pathogenic species by increasing its relative propensity to form prefibrillar but not fibrillar aggregates, and, conversely, to abolish the pathogenicity of the highly neurotoxic E22G Aβ42 peptide by reducing its relative propensity to form prefibrillar species rather than mature fibrillar ones. This observation can be rationalized by the demonstration that whereas regions of the sequence of high aggregation propensity dominate the overall tendency to aggregate, regions with low intrinsic aggregation propensities exert significant control over the balance of the prefibrillar and fibrillar species formed, and therefore play a major role in determining the neurotoxicity of the Aβ peptide. © 2010 by the Biophysical Society
A metastable subproteome underlies inclusion formation in muscle proteinopathies
Protein aggregation is a pathological feature of neurodegenerative disorders. We previously demonstrated that protein inclusions in the brain are composed of supersaturated proteins, which are abundant and aggregation-prone, and form a metastable subproteome. It is not yet clear, however, whether this phenomenon is also associated with non-neuronal protein conformational disorders. To respond to this question, we analyzed proteomic datasets from biopsies of patients with genetic and acquired protein aggregate myopathy (PAM) by quantifying the changes in composition, concentration and aggregation propensity of proteins in the fibers containing inclusions and those surrounding them. We found that a metastable subproteome is present in skeletal muscle from healthy patients. The expression of this subproteome escalate as proteomic samples are taken more proximal to the pathologic inclusion, eventually exceeding its solubility limits and aggregating. While most supersaturated proteins decrease or maintain steady abundance across healthy fibers and inclusion-containing fibers, proteins within the metastable subproteome rise in abundance, suggesting that they escape regulation. Taken together, our results show in the context of a human conformational disorder that the supersaturation of a metastable subproteome underlies widespread aggregation and correlates with the histopathological state of the tissue
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