126 research outputs found
Has the density of sources of gamma-ray burts been constant over the last ten billion years ?
A generic tired-light mechanism is examined in which a photon, like any
particle moving in a medium, experiences friction, that is, a force resisting
its motion. If the velocity of light is assumed to be constant, this hypothesis
yields a Hubble-like law which is also a consequence of the Rh = ct cosmology.
Herein, it is used for estimating matter density as a function of redshift,
allowing to show that the density of sources of long gamma-ray bursts appears
to be nearly constant, up to z 4. Assuming that the later is a fair
probe of the former, this means that matter density has been roughly constant
over the last ten billion years, implying that, at least over this period,
matter has been in an overall state of equilibrium.Comment: 5 pages, 1 figur
On the unknown proteins of eukaryotic proteomes
In order to study unknown proteins on a large scale, a reference system has
been set up for the three major eukaryotic lineages, built with 36 proteomes as
taxonomically diverse as possible. Proteins from 362 eukaryotic proteomes with
no known homologue in this set were then analyzed, focusing noteworthy on
singletons, that is, on unknown proteins with no known homologue in their own
proteome. Consistently, according to Uniprot, for a given species, no more than
12% of the singletons thus found are known at the protein level. Also, since
they rely on the information found in the alignment of homologous sequences,
predictions of AlphaFold2 for their tridimensional structure are usually poor.
In the case of metazoan species, the number of singletons seems to increase as
a function of the evolutionary distance from the reference system.
Interestingly, no such trend is found in the cases of viridiplantae and fungi,
as if the timescale on which singletons are added to proteomes were different
in metazoa and in other eukaryotic kingdoms. In order to confirm this
phenomenon, further studies of proteomes closer to those of the reference
system are however needed.Comment: 11 pages, 5 figure
Discrete breathers in nonlinear network models of proteins
We introduce a topology-based nonlinear network model of protein dynamics
with the aim of investigating the interplay of spatial disorder and
nonlinearity. We show that spontaneous localization of energy occurs
generically and is a site-dependent process. Localized modes of nonlinear
origin form spontaneously in the stiffest parts of the structure and display
site-dependent activation energies. Our results provide a straightforward way
for understanding the recently discovered link between protein local stiffness
and enzymatic activity. They strongly suggest that nonlinear phenomena may play
an important role in enzyme function, allowing for energy storage during the
catalytic process.Comment: 4 pages, 5 figures. Minor change
Slow energy relaxation of macromolecules and nano-clusters in solution
Many systems in the realm of nanophysics from both the living and inorganic
world display slow relaxation kinetics of energy fluctuations. In this paper we
propose a general explanation for such phenomenon, based on the effects of
interactions with the solvent. Within a simple harmonic model of the system
fluctuations, we demonstrate that the inhomogeneity of coupling to the solvent
of the bulk and surface atoms suffices to generate a complex spectrum of decay
rates. We show for Myoglobin and for a metal nano-cluster that the result is a
complex, non-exponential relaxation dynamics.Comment: 5 pages, 3 figure
ΠΠ°ΠΊΡΠΎΠ΅ΠΊΠΎΠ½ΠΎΠΌΡΡΠ½Ρ ΠΏΡΠΎΠ±Π»Π΅ΠΌΠΈ ΡΠ½ΡΠ»ΡΡΡΡ Π² ΡΠΌΠΎΠ²Π°Ρ Π΅ΠΊΠΎΠ½ΠΎΠΌΡΡΠ½ΠΎΡ ΡΡΠ°Π½ΡΡΠΎΡΠΌΠ°ΡΡΡ
Π ΠΎΠ·Π³Π»ΡΠ½ΡΡΠΎ ΠΏΡΠΎΠ±Π»Π΅ΠΌΡ ΡΠ½ΡΠ»ΡΡΡΡ ΡΠΊ ΡΡΠ½Π΄Π°ΠΌΠ΅Π½ΡΠ°Π»ΡΠ½Ρ ΠΏΡΠΎΠ±Π»Π΅ΠΌΡ Π΄Π»Ρ ΡΠΎΠ·Π²ΠΈΡΠΊΡ Π±ΡΠ΄Ρ-ΡΠΊΠΎΡ ΠΊΡΠ°ΡΠ½ΠΈ. Π‘ΡΠ²Π΅ΡΠ΄ΠΆΠ΅Π½ΠΎ, ΡΠΎ Π² Π΅ΠΊΠΎΠ½ΠΎΠΌΡΡΠ½ΡΠΉ Π½Π°ΡΡΡ Π½Π΅ ΡΡΠ½ΡΡ ΡΠ΄ΠΈΠ½ΠΈΡ
ΠΏΡΠ΄Ρ
ΠΎΠ΄ΡΠ² ΡΠΎΠ΄ΠΎ ΡΡΡΡ ΡΡΠΎΠ³ΠΎ ΡΠ²ΠΈΡΠ°, ΠΏΡΠΈΡΠΈΠ½ ΠΏΠΎΡΠ²ΠΈ Ρ Π½Π°ΡΠ»ΡΠ΄ΠΊΡΠ², Π° ΡΠ°ΠΊΠΎΠΆ ΠΎΡΠ½ΠΎΠ²Π½ΠΈΡ
Π½Π°ΠΏΡΡΠΌΡΠ² Π±ΠΎΡΠΎΡΡΠ±ΠΈ Π· ΡΠ½ΡΠ»ΡΡΡΡΡ. ΠΠ°ΠΊΡΠΎΠ΅ΠΊΠΎΠ½ΠΎΠΌΡΡΠ½ΠΈΠΉ ΡΠ½ΡΠ»ΡΡΡΠΉΠ½ΠΈΠΉ Π²ΠΏΠ»ΠΈΠ² Π½Π° Π΅ΠΊΠΎΠ½ΠΎΠΌΡΠΊΡ ΠΌΠ°Ρ ΡΠ²ΠΎΡ ΡΠΏΠ΅ΡΠΈΡΡΠΊΡ Π² ΡΠΌΠΎΠ²Π°Ρ
ΡΠΎΡΠΌΡΠ²Π°Π½Π½Ρ ΡΠΈΠ½ΠΊΠΎΠ²ΠΈΡ
Π²ΡΠ΄Π½ΠΎΡΠΈΠ½ ΠΊΡΠ°ΡΠ½ ΠΏΠ΅ΡΠ΅Ρ
ΡΠ΄Π½ΠΎΡ Π΅ΠΊΠΎΠ½ΠΎΠΌΡΠΊΠΈ (Π½Π°ΠΏΡΠΈΠΊΠ»Π°Π΄, Π£ΠΊΡΠ°ΡΠ½ΠΈ). Π Π·Π°ΡΡΠΎΡΡΠ²Π°Π½Π½ΡΠΌ ΠΌΠ΅ΡΠΎΠ΄ΠΎΠ»ΠΎΠ³ΡΡ ΡΡΠ½ΠΊΡΡΠΎΠ½Π°Π»ΡΠ½ΠΎΠ³ΠΎ Π°Π½Π°Π»ΡΠ·Ρ, ΡΠΈΡΡΠ΅ΠΌΠ½ΠΎΠ³ΠΎ ΠΏΡΠ΄Ρ
ΠΎΠ΄Ρ ΡΠ° Π°Π½Π°Π»ΠΎΠ³ΡΡ ΠΏΡΠΎΠ°Π½Π°Π»ΡΠ·ΠΎΠ²Π°Π½ΠΎ ΠΏΡΠΈΡΠΈΠ½ΠΈ Ρ Π½Π°ΡΠ»ΡΠ΄ΠΊΠΈ ΡΠ½ΡΠ»ΡΡΡΡ, Π°Π½ΡΠΈΡΠ½ΡΠ»ΡΡΡΠΉΠ½Ρ ΠΏΠΎΠ»ΡΡΠΈΠΊΡ, ΡΠΊΠ° ΠΏΡΠΎΠ²ΠΎΠ΄ΠΈΡΡΡΡ Π² ΡΠΌΠΎΠ²Π°Ρ
ΡΠΈΠ½ΠΊΠΎΠ²ΠΎΡ Π΅ΠΊΠΎΠ½ΠΎΠΌΡΠΊΠΈ. ΠΡΠΎΠ±Π»ΠΈΠ²Ρ ΡΠ²Π°Π³Ρ Π·Π²Π΅ΡΠ½Π΅Π½ΠΎ Π½Π° ΠΌΠ°ΠΊΡΠΎΠ΅ΠΊΠΎΠ½ΠΎΠΌΡΡΠ½Ρ ΠΏΡΠΎΠ±Π»Π΅ΠΌΠΈ ΡΠ½ΡΠ»ΡΡΡΡ Π² Π΅ΠΊΠΎΠ½ΠΎΠΌΡΡΡ ΡΡΡΠ°ΡΠ½ΠΎΡ Π£ΠΊΡΠ°ΡΠ½ΠΈ. ΠΡΠΎΠ±Π»Π΅Π½ΠΎ Π²ΠΈΡΠ½ΠΎΠ²ΠΊΠΈ ΠΏΡΠΎ Π½Π΅ΠΎΠ±Ρ
ΡΠ΄Π½ΡΡΡΡ ΠΏΡΠΎΠ²Π΅Π΄Π΅Π½Π½Ρ Π²ΠΈΠ²Π°ΠΆΠ΅Π½ΠΈΡ
ΡΠΊ ΠΏΠΎΠ»ΡΡΠΈΡΠ½ΠΈΡ
, ΡΠ°ΠΊ Ρ Π΅ΠΊΠΎΠ½ΠΎΠΌΡΡΠ½ΠΈΡ
ΡΡΡΠ΅Π½Ρ, Π²ΡΠ΄ ΡΠΊΠΈΡ
Π·Π°Π»Π΅ΠΆΠΈΡΡ ΠΌΠ°ΠΉΠ±ΡΡΠ½Ρ Π΅ΠΊΠΎΠ½ΠΎΠΌΡΠΊΠΈ Π½Π°ΡΠΎΡ Π΄Π΅ΡΠΆΠ°Π²ΠΈ.Π Π°ΡΡΠΌΠΎΡΡΠ΅Π½Π° ΠΏΡΠΎΠ±Π»Π΅ΠΌΠ° ΠΈΠ½ΡΠ»ΡΡΠΈΠΈ ΠΊΠ°ΠΊ ΡΡΠ½Π΄Π°ΠΌΠ΅Π½ΡΠ°Π»ΡΠ½ΡΡ ΠΏΡΠΎΠ±Π»Π΅ΠΌΡ Π΄Π»Ρ ΡΠ°Π·Π²ΠΈΡΠΈΡ Π»ΡΠ±ΠΎΠΉ ΡΡΡΠ°Π½Ρ. Π£ΡΠ²Π΅ΡΠΆΠ΄Π΅Π½ΠΎ, ΡΡΠΎ Π² ΡΠΊΠΎΠ½ΠΎΠΌΠΈΡΠ΅ΡΠΊΠΎΠΉ Π½Π°ΡΠΊΠ΅ Π½Π΅ ΡΡΡΠ΅ΡΡΠ²ΡΠ΅Ρ Π΅Π΄ΠΈΠ½ΡΡ
ΠΏΠΎΠ΄Ρ
ΠΎΠ΄ΠΎΠ² ΠΊ ΡΡΡΠΈ ΡΡΠΎΠ³ΠΎ ΡΠ²Π»Π΅Π½ΠΈΡ, ΠΏΡΠΈΡΠΈΠ½ ΠΏΠΎΡΠ²Π»Π΅Π½ΠΈΡ ΠΈ ΠΏΠΎΡΠ»Π΅Π΄ΡΡΠ²ΠΈΠΉ, Π° ΡΠ°ΠΊΠΆΠ΅ ΠΎΡΠ½ΠΎΠ²Π½ΡΡ
Π½Π°ΠΏΡΠ°Π²Π»Π΅Π½ΠΈΠΉ Π±ΠΎΡΡΠ±Ρ Ρ ΠΈΠ½ΡΠ»ΡΡΠΈΠ΅ΠΉ. ΠΠ°ΠΊΡΠΎΡΠΊΠΎΠ½ΠΎΠΌΠΈΡΠ΅ΡΠΊΠΈΠΉ ΠΈΠ½ΡΠ»ΡΡΠΈΠΎΠ½Π½ΠΎΠ΅ Π²ΠΎΠ·Π΄Π΅ΠΉΡΡΠ²ΠΈΠ΅ Π½Π° ΡΠΊΠΎΠ½ΠΎΠΌΠΈΠΊΡ ΠΈΠΌΠ΅Π΅Ρ ΡΠ²ΠΎΡ ΡΠΏΠ΅ΡΠΈΡΠΈΠΊΡ Π² ΡΡΠ»ΠΎΠ²ΠΈΡΡ
ΡΠΎΡΠΌΠΈΡΠΎΠ²Π°Π½ΠΈΡ ΡΡΠ½ΠΎΡΠ½ΡΡ
ΠΎΡΠ½ΠΎΡΠ΅Π½ΠΈΠΉ ΡΡΡΠ°Π½ ΠΏΠ΅ΡΠ΅Ρ
ΠΎΠ΄Π½ΠΎΠΉ ΡΠΊΠΎΠ½ΠΎΠΌΠΈΠΊΠΈ (Π½Π°ΠΏΡΠΈΠΌΠ΅Ρ, Π£ΠΊΡΠ°ΠΈΠ½Π°). ΠΡΠΈΠΌΠ΅Π½Π΅Π½ΠΈΠ΅ ΠΌΠ΅ΡΠΎΠ΄ΠΎΠ»ΠΎΠ³ΠΈΠΈ ΡΡΠ½ΠΊΡΠΈΠΎΠ½Π°Π»ΡΠ½ΠΎΠ³ΠΎ Π°Π½Π°Π»ΠΈΠ·Π°, ΡΠΈΡΡΠ΅ΠΌΠ½ΠΎΠ³ΠΎ ΠΏΠΎΠ΄Ρ
ΠΎΠ΄Π° ΠΈ Π°Π½Π°Π»ΠΎΠ³ΠΈΠΈ ΠΏΡΠΎΠ°Π½Π°Π»ΠΈΠ·ΠΈΡΠΎΠ²Π°Π½Ρ Π°Π½Π°Π»ΠΈΠ·ΠΈΡΡΡΡΡΡ ΠΏΡΠΈΡΠΈΠ½Ρ ΠΈ ΠΏΠΎΡΠ»Π΅Π΄ΡΡΠ²ΠΈΡ ΠΈΠ½ΡΠ»ΡΡΠΈΠΈ, Π°Π½ΡΠΈΠΈΠ½ΡΠ»ΡΡΠΈΠΎΠ½Π½ΡΡ ΠΏΠΎΠ»ΠΈΡΠΈΠΊΡ, ΠΊΠΎΡΠΎΡΠ°Ρ ΠΏΡΠΎΠ²ΠΎΠ΄ΠΈΡΡΡ Π² ΡΡΠ»ΠΎΠ²ΠΈΡΡ
ΡΡΠ½ΠΎΡΠ½ΠΎΠΉ ΡΠΊΠΎΠ½ΠΎΠΌΠΈΠΊΠΈ. ΠΡΠΎΠ±ΠΎΠ΅ Π²Π½ΠΈΠΌΠ°Π½ΠΈΠ΅ ΠΎΠ±ΡΠ°ΡΠ΅Π½ΠΎ Π½Π° ΠΌΠ°ΠΊΡΠΎΡΠΊΠΎΠ½ΠΎΠΌΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΏΡΠΎΠ±Π»Π΅ΠΌΡ ΠΈΠ½ΡΠ»ΡΡΠΈΠΈ Π² ΡΠΊΠΎΠ½ΠΎΠΌΠΈΠΊΠ΅ ΡΠΎΠ²ΡΠ΅ΠΌΠ΅Π½Π½ΠΎΠΉ Π£ΠΊΡΠ°ΠΈΠ½Ρ. Π‘Π΄Π΅Π»Π°Π½Ρ Π²ΡΠ²ΠΎΠ΄Ρ ΠΎ Π½Π΅ΠΎΠ±Ρ
ΠΎΠ΄ΠΈΠΌΠΎΡΡΠΈ ΠΏΡΠΎΠ²Π΅Π΄Π΅Π½ΠΈΡ Π²Π·Π²Π΅ΡΠ΅Π½Π½ΡΡ
ΠΊΠ°ΠΊ ΠΏΠΎΠ»ΠΈΡΠΈΡΠ΅ΡΠΊΠΈΡ
, ΡΠ°ΠΊ ΠΈ ΡΠΊΠΎΠ½ΠΎΠΌΠΈΡΠ΅ΡΠΊΠΈΡ
ΡΠ΅ΡΠ΅Π½ΠΈΠΉ, ΠΎΡ ΠΊΠΎΡΠΎΡΡΡ
Π·Π°Π²ΠΈΡΠΈΡ Π±ΡΠ΄ΡΡΠ΅Π΅ ΡΠΊΠΎΠ½ΠΎΠΌΠΈΠΊΠΈ Π³ΠΎΡΡΠ΄Π°ΡΡΡΠ²Π°.Inflation is a fundamental problem for the development of any country. There are no common approaches to the nature, causes and consequences of this phenomenon and the ways of its reduction in economics. Macroeconomical inflation impact on the economy has its own distinctive aspects in terms of the building of marketing relationships in the countries with transition economy (Ukraine, for example). Using methods of functional analysis, system analysis and analogy method the causes and consequences of inflation as well as antiinflationary policy conducted in a market economy are analyzed in the article. Special attention is paid to macro-economical problems of inflation in the economy of modern Ukraine. The conclusion about the necessity of making the deliberated political and economical decisions that affect the future economy of our country is made
Functional modes of proteins are among the most robust ones
It is shown that a small subset of modes which are likely to be involved in
protein functional motions of large amplitude can be determined by retaining
the most robust normal modes obtained using different protein models. This
result should prove helpful in the context of several applications proposed
recently, like for solving difficult molecular replacement problems or for
fitting atomic structures into low-resolution electron density maps. Moreover,
it may also pave the way for the development of methods allowing to predict
such motions accurately.Comment: 4 pages, 5 figure
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