96 research outputs found
Multiexcitons confined within a sub-excitonic volume: Spectroscopic and dynamical signatures of neutral and charged biexcitons in ultrasmall semiconductor nanocrystals
The use of ultrafast gating techniques allows us to resolve both spectrally
and temporally the emission from short-lived neutral and negatively charged
biexcitons in ultrasmall (sub-10 nm) CdSe nanocrystals (nanocrystal quantum
dots). Because of forced overlap of electronic wave functions and reduced
dielectric screening, these states are characterized by giant interaction
energies of tens (neutral biexcitons) to hundreds (charged biexcitons) of meV.
Both types of biexcitons show extremely short lifetimes (from sub-100
picoseconds to sub-picosecond time scales) that rapidly shorten with decreasing
nanocrystal size. These ultrafast relaxation dynamics are explained in terms of
highly efficient nonradiative Auger recombination.Comment: 5 pages, 4 figures, to be published in Phys. Rev.
Macromolecular crowding modulates folding mechanism of alpha/beta protein apoflavodoxin
Protein dynamics in cells may be different from that in dilute solutions in
vitro since the environment in cells is highly concentrated with other
macromolecules. This volume exclusion due to macromolecular crowding is
predicted to affect both equilibrium and kinetic processes involving protein
conformational changes. To quantify macromolecular crowding effects on protein
folding mechanisms, here we have investigated the folding energy landscape of
an alpha/beta protein, apoflavodoxin, in the presence of inert macromolecular
crowding agents using in silico and in vitro approaches. By coarse-grained
molecular simulations and topology-based potential interactions, we probed the
effects of increased volume fraction of crowding agents (phi_c) as well as of
crowding agent geometry (sphere or spherocylinder) at high phi_c. Parallel
kinetic folding experiments with purified Desulfovibro desulfuricans
apoflavodoxin in vitro were performed in the presence of Ficoll (sphere) and
Dextran (spherocylinder) synthetic crowding agents. In conclusion, we have
identified in silico crowding conditions that best enhance protein stability
and discovered that upon manipulation of the crowding conditions, folding
routes experiencing topological frustrations can be either enhanced or
relieved. The test-tube experiments confirmed that apoflavodoxin's
time-resolved folding path is modulated by crowding agent geometry. We propose
that macromolecular crowding effects may be a tool for manipulation of protein
folding and function in living cells.Comment: to appear in Biophysical Journal (2009). to appear in Biophysical
Journal (2009
Постать Тараса Шевченка в рецепції Ліни Костенко
У статті розглядається поетика творення Ліною Костенко образу Кобзаря крізь призму власного "я", через пережиті відчуття поета-шістдесятника, що своєю проекцією нагадують душевні терзання великого поета.В статье рассмотрена поэтика создания Линой Костенко образа Тараса Шевченко сквозь призму собственного "я", через пережитые ощущения поэта-шестидесятника, своей проекцией напоминающие душевные терзания великого поэта.The article deals with the problem of the poetics creation by Lina Kostenko Taras Shevchenko’ image through a prism her own mind, through sensations of the poet-sixtier, by the projection reminding sincere torments the great poet is considered
Folding, Stability and Shape of Proteins in Crowded Environments: Experimental and Computational Approaches
How the crowded environment inside cells affects folding, stability and structures of proteins is a vital question, since most proteins are made and function inside cells. Here we describe how crowded conditions can be created in vitro and in silico and how we have used this to probe effects on protein properties. We have found that folded forms of proteins become more compact in the presence of macromolecular crowding agents; if the protein is aspherical, the shape also changes (extent dictated by native-state stability and chemical conditions). It was also discovered that the shape of the macromolecular crowding agent modulates the folding mechanism of a protein; in addition, the extent of asphericity of the protein itself is an important factor in defining its folding speed
Folding Circular Permutants of IL-1β: Route Selection Driven by Functional Frustration
Interleukin-1β (IL-1β) is the cytokine crucial to inflammatory and immune response. Two dominant routes are populated in the folding to native structure. These distinct routes are a result of the competition between early packing of the functional loops versus closure of the β-barrel to achieve efficient folding and have been observed both experimentally and computationally. Kinetic experiments on the WT protein established that the dominant route is characterized by early packing of geometrically frustrated functional loops. However, deletion of one of the functional loops, the β-bulge, switches the dominant route to an alternative, yet, as accessible, route, where the termini necessary for barrel closure form first. Here, we explore the effect of circular permutation of the WT sequence on the observed folding landscape with a combination of kinetic and thermodynamic experiments. Our experiments show that while the rate of formation of permutant protein is always slower than that observed for the WT sequence, the region of initial nucleation for all permutants is similar to that observed for the WT protein and occurs within a similar timescale. That is, even permutants with significant sequence rearrangement in which the functional-nucleus is placed at opposing ends of the polypeptide chain, fold by the dominant WT “functional loop-packing route”, despite the entropic cost of having to fold the N- and C- termini early. Taken together, our results indicate that the early packing of the functional loops dominates the folding landscape in active proteins, and, despite the entropic penalty of coalescing the termini early, these proteins will populate an entropically unfavorable route in order to conserve function. More generally, circular permutation can elucidate the influence of local energetic stabilization of functional regions within a protein, where topological complexity creates a mismatch between energetics and topology in active proteins
Capillary electrophoretic separation of nanoparticles
In the present work, CdSe nanocrystals (NCs) synthesized with a trioctylphosphine surface passivation layer were modified using amphiphilic molecules to form a surface bilayer capable of providing stable NCs aqueous solutions. Such modified nanocrystals were used as a test solute in order to analyze new electrophoretic phenomena, by applying a micellar plug as a separation tool for discriminating nanocrystals between micellar and micelle-free zones during electrophoresis. The distribution of NCs between both zones depended on the affinity of nanocrystals towards the micellar zone, and this relies on the kind of surface ligands attached to the NCs, as well as electrophoretic conditions applied. In this case, the NCs that migrated within a micellar zone can be focused using a preconcentration mechanism. By modifying electrophoretic conditions, NCs were forced to migrate outside the micellar zone in the form of a typical CZE peak. In this situation, a two-order difference in separation efficiencies, in terms of theoretical plates, was observed between focused NCs (N ~ 107) and a typical CZE peak for NCs (N ~ 105). By applying the amino-functionalized NCs the preconcentration of NCs, using a micellar plug, was examined, with the conclusion that preconcentration efficiency, in terms of the enhancement factor for peak height (SEFheight) can be, at least 20. The distribution effect was applied to separate CdSe/ZnS NCs encapsulated in silica, as well as surface-modified with DNA, which allows the estimation of the yield of conjugation of biologically active molecules to a particle surface
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