1,295 research outputs found
System description and operating guide for DSAS illumination and moon conflict programs
The DSAS Illumination and Moon Conflict programs are described which during an orbit when the DSAS (Digital Solar Aspect Sensor) will record the direct rays of the sun, and the periods of time when the horizon scanners will come in conflict with the moon. The DSAS Illumination Program makes use of an orbit tape (or epoch time and orbital elements) in addition to an ephemeris tape containing positions of the sun and moon. The Moon Conflict Program makes use of the same ephemeris tape with sun and moon positions, but uses only epoch time and orbital elements for the satellite positions. These programs were designed for the TIROS or ITOS series spacecraft but may be utilized by any spacecraft with similar sensors
Influence of the heterointerface sharpness on exciton recombination dynamics in an ensemble of (In,Al)As/AlAs quantum dots with indirect band-gap
The dynamics of exciton recombination in an ensemble of indirect band-gap
(In,Al)As/AlAs quantum dots with type-I band alignment is studied. The lifetime
of confined excitons which are indirect in momentum-space is mainly influenced
by the sharpness of the heterointerface between the (In,Al)As quantum dot and
the AlAs barrier matrix. Time-resolved photoluminescence experiments and
theoretical model calculations reveal a strong dependence of the exciton
lifetime on the thickness of the interface diffusion layer. The lifetime of
excitons with a particular optical transition energy varies because this energy
is obtained for quantum dots differing in size, shape and composition. The
different exciton lifetimes, which result in photoluminescence with
non-exponential decay obeying a power-law function, can be described by a
phenomenological distribution function, which allows one to explain the
photoluminescence decay with one fitting parameter only.Comment: 10 pages, 7 figure
Widespread recombination, reassortment, and transmission of unbalanced compound viral genotypes in natural arenavirus infections.
Arenaviruses are one of the largest families of human hemorrhagic fever viruses and are known to infect both mammals and snakes. Arenaviruses package a large (L) and small (S) genome segment in their virions. For segmented RNA viruses like these, novel genotypes can be generated through mutation, recombination, and reassortment. Although it is believed that an ancient recombination event led to the emergence of a new lineage of mammalian arenaviruses, neither recombination nor reassortment has been definitively documented in natural arenavirus infections. Here, we used metagenomic sequencing to survey the viral diversity present in captive arenavirus-infected snakes. From 48 infected animals, we determined the complete or near complete sequence of 210 genome segments that grouped into 23 L and 11 S genotypes. The majority of snakes were multiply infected, with up to 4 distinct S and 11 distinct L segment genotypes in individual animals. This S/L imbalance was typical: in all cases intrahost L segment genotypes outnumbered S genotypes, and a particular S segment genotype dominated in individual animals and at a population level. We corroborated sequencing results by qRT-PCR and virus isolation, and isolates replicated as ensembles in culture. Numerous instances of recombination and reassortment were detected, including recombinant segments with unusual organizations featuring 2 intergenic regions and superfluous content, which were capable of stable replication and transmission despite their atypical structures. Overall, this represents intrahost diversity of an extent and form that goes well beyond what has been observed for arenaviruses or for viruses in general. This diversity can be plausibly attributed to the captive intermingling of sub-clinically infected wild-caught snakes. Thus, beyond providing a unique opportunity to study arenavirus evolution and adaptation, these findings allow the investigation of unintended anthropogenic impacts on viral ecology, diversity, and disease potential
The N-terminal intrinsically disordered domain of mgm101p is localized to the mitochondrial nucleoid.
The mitochondrial genome maintenance gene, MGM101, is essential for yeasts that depend on mitochondrial DNA replication. Previously, in Saccharomyces cerevisiae, it has been found that the carboxy-terminal two-thirds of Mgm101p has a functional core. Furthermore, there is a high level of amino acid sequence conservation in this region from widely diverse species. By contrast, the amino-terminal region, that is also essential for function, does not have recognizable conservation. Using a bioinformatic approach we find that the functional core from yeast and a corresponding region of Mgm101p from the coral Acropora millepora have an ordered structure, while the N-terminal domains of sequences from yeast and coral are predicted to be disordered. To examine whether ordered and disordered domains of Mgm101p have specific or general functions we made chimeric proteins from yeast and coral by swapping the two regions. We find, by an in vivo assay in S.cerevisiae, that the ordered domain of A.millepora can functionally replace the yeast core region but the disordered domain of the coral protein cannot substitute for its yeast counterpart. Mgm101p is found in the mitochondrial nucleoid along with enzymes and proteins involved in mtDNA replication. By attaching green fluorescent protein to the N-terminal disordered domain of yeast Mgm101p we find that GFP is still directed to the mitochondrial nucleoid where full-length Mgm101p-GFP is targeted
The Supremum Norm of the Discrepancy Function: Recent Results and Connections
A great challenge in the analysis of the discrepancy function D_N is to
obtain universal lower bounds on the L-infty norm of D_N in dimensions d \geq
3. It follows from the average case bound of Klaus Roth that the L-infty norm
of D_N is at least (log N) ^{(d-1)/2}. It is conjectured that the L-infty bound
is significantly larger, but the only definitive result is that of Wolfgang
Schmidt in dimension d=2. Partial improvements of the Roth exponent (d-1)/2 in
higher dimensions have been established by the authors and Armen Vagharshakyan.
We survey these results, the underlying methods, and some of their connections
to other subjects in probability, approximation theory, and analysis.Comment: 15 pages, 3 Figures. Reports on talks presented by the authors at the
10th international conference on Monte Carlo and Quasi-Monte Carlo Methods in
Scientific Computing, Sydney Australia, February 2011. v2: Comments of the
referee are incorporate
Body image, cosmesis, quality of life, and functional outcome of hand-assisted laparoscopic versus open restorative proctocolectomy: long-term results of a randomized trial
BACKGROUND: This study aimed to compare quality of life (QOL), functional outcome, body image, and cosmesis after hand-assisted laparoscopic (LRP) versus open restorative proctocolectomy (ORP). The potential long-term advantages of LRP over ORP remain to be determined. The most likely advantage of LRP is the superior cosmetic result. It is, however, unclear whether the size and location of incisions affect body image and QOL. METHODS: In a previously conducted randomized trial comparing LRP with ORP, 60 patients were prospectively evaluated. The primary end points were body image and cosmesis. The secondary end points were morbidity, QOL, and functional outcome. A body image questionnaire was used to evaluate body image and cosmesis. The Short Form-36 Health Survey and the Gastrointestinal Quality of Life Inventory were used to assess QOL. Body image and QOL also were assessed preoperatively. RESULTS: A total of 53 patients completed the QOL and functional outcome questionnaires. There were no differences in functional outcome, morbidity, or QOL between LRP and ORP. At a median of 2.7 years after surgery, 46 patients returned the questionnaires regarding body image, cosmesis, and morbidity. The body image and cosmesis scores of female patients were significantly higher in the LRP group than in the ORP group (body image, 17.4 vs 14.9; cosmesis, 19.1 vs 13.0, respectively). The female patients in the ORP group had significantly lower body image scores than the male patients (14.9 vs 18.3). CONCLUSIONS: This study is the first to show that ORP has a negative impact on body image and cosmesis as compared with LRP. Functional outcome, QOL, and morbidity are similar for the two approaches. The advantages of a long-lasting improved body image and cosmesis for this relatively young patient population may compensate for the longer operating times and higher costs, particularly for wome
Polycation-π Interactions Are a Driving Force for Molecular Recognition by an Intrinsically Disordered Oncoprotein Family
Molecular recognition by intrinsically disordered proteins (IDPs) commonly involves specific localized contacts and target-induced disorder to order transitions. However, some IDPs remain disordered in the bound state, a phenomenon coined "fuzziness", often characterized by IDP polyvalency, sequence-insensitivity and a dynamic ensemble of disordered bound-state conformations. Besides the above general features, specific biophysical models for fuzzy interactions are mostly lacking. The transcriptional activation domain of the Ewing's Sarcoma oncoprotein family (EAD) is an IDP that exhibits many features of fuzziness, with multiple EAD aromatic side chains driving molecular recognition. Considering the prevalent role of cation-π interactions at various protein-protein interfaces, we hypothesized that EAD-target binding involves polycation- π contacts between a disordered EAD and basic residues on the target. Herein we evaluated the polycation-π hypothesis via functional and theoretical interrogation of EAD variants. The experimental effects of a range of EAD sequence variations, including aromatic number, aromatic density and charge perturbations, all support the cation-π model. Moreover, the activity trends observed are well captured by a coarse-grained EAD chain model and a corresponding analytical model based on interaction between EAD aromatics and surface cations of a generic globular target. EAD-target binding, in the context of pathological Ewing's Sarcoma oncoproteins, is thus seen to be driven by a balance between EAD conformational entropy and favorable EAD-target cation-π contacts. Such a highly versatile mode of molecular recognition offers a general conceptual framework for promiscuous target recognition by polyvalent IDPs. © 2013 Song et al
Discrete molecular dynamics can predict helical prestructured motifs in disordered proteins.
Intrinsically disordered proteins (IDPs) lack a stable tertiary structure, but their short binding regions termed Pre-Structured Motifs (PreSMo) can form transient secondary structure elements in solution. Although disordered proteins are crucial in many biological processes and designing strategies to modulate their function is highly important, both experimental and computational tools to describe their conformational ensembles and the initial steps of folding are sparse. Here we report that discrete molecular dynamics (DMD) simulations combined with replica exchange (RX) method efficiently samples the conformational space and detects regions populating alpha-helical conformational states in disordered protein regions. While the available computational methods predict secondary structural propensities in IDPs based on the observation of protein-protein interactions, our ab initio method rests on physical principles of protein folding and dynamics. We show that RX-DMD predicts alpha-PreSMos with high confidence confirmed by comparison to experimental NMR data. Moreover, the method also can dissect alpha-PreSMos in close vicinity to each other and indicate helix stability. Importantly, simulations with disordered regions forming helices in X-ray structures of complexes indicate that a preformed helix is frequently the binding element itself, while in other cases it may have a role in initiating the binding process. Our results indicate that RX-DMD provides a breakthrough in the structural and dynamical characterization of disordered proteins by generating the structural ensembles of IDPs even when experimental data are not available
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