Binary Pulsar Tests of General Relativity in the Presence of Low-Frequency Noise

The influence of the low-frequency timing noise on the precision of measurements of the Keplerian and post-Keplerian orbital parameters in binary pulsars is studied. Fundamental limits on the accuracy of tests of alternative theories of gravity in the strong-field regime are established. The gravitational low-frequency timing noise formed by an ensemble of binary stars is briefly discussed.Comment: 4 pages, contributed paper to the proceedings of the IAU167 colloquium on pulsars, Bonn, August-September 199

Synthesis of New Bitopic Tetra(pyrazolyl)-Ligands with Neopentane and O-Xylene Backbones

Several new bitopic pyrazole-containing ligands were prepared from the corresponding pyrazoles and tetrahalogen or tetratosyloxy derivatives of o-xylene and neopentane in a superbasic medium (KOH-DMSO)

Pharmacological correction of intrarenal hemodynamic disorders in acute kidney injury (part 2)

Evaluate the possibilities of individual pharmacological correction and intensive care of patients with acute kidney injury of different origin. A prospective nonrandomized study. Inclusion criteria: patients with prerenal, renal and subrenal AKI module in stage of oligoanuria and restoration of diuresis. Exclusion criteria: AKI in patients after cardiosurgery and operations on large vessels. Individual pharmacological and non-pharmacological correction (renoprotection) was performed in 250 ICU patients with prerenal (130), renal (81) and subrenal (39) AK

Bitangential interpolation in generalized Schur classes

Bitangential interpolation problems in the class of matrix valued functions in the generalized Schur class are considered in both the open unit disc and the open right half plane, including problems in which the solutions is not assumed to be holomorphic at the interpolation points. Linear fractional representations of the set of solutions to these problems are presented for invertible and singular Hermitian Pick matrices. These representations make use of a description of the ranges of linear fractional transformations with suitably chosen domains that was developed in a previous paper.Comment: Second version, corrected typos, changed subsection 5.6, 47 page

In vitro terahertz spectroscopy of gelatin-embedded human brain tumors - a pilot study

We have performed the in vitro terahertz (THz) spectroscopy of human brain tumors. In order to x tissue

Therminator DNA Polymerase: Modified Nucleotides and Unnatural Substrates

A variant of 9°N DNA polymerase [Genbank ID (AAA88769.1)] with three mutations (D141A, E143A, A485L) and commercialized under the name “Therminator DNA polymerase” has the ability to incorporate a variety of modified nucleotide classes. This Review focuses on how Therminator DNA Polymerase has enabled new technologies in synthetic biology and DNA sequencing. In addition, we discuss mechanisms for increased modified nucleotide incorporation

Millisecond and Binary Pulsars as Nature's Frequency Standards. III. Fourier Analysis and Spectral Sensitivity of Timing Observations to Low-Frequency Noise

This paper discusses spectral sensitivity of solitary and binary pulsars to a low-frequency (colored) noise. It is a third paper in a series of papers devoted to analysis of the low-frequency noise in pulsar timing observations and its impact on observable fitting parameters of timing model.Comment: 25 pages, 3 figures, accepted to MNRA

Anchored Design of Protein-Protein Interfaces

Few existing protein-protein interface design methods allow for extensive backbone rearrangements during the design process. There is also a dichotomy between redesign methods, which take advantage of the native interface, and de novo methods, which produce novel binders.Here, we propose a new method for designing novel protein reagents that combines advantages of redesign and de novo methods and allows for extensive backbone motion. This method requires a bound structure of a target and one of its natural binding partners. A key interaction in this interface, the anchor, is computationally grafted out of the partner and into a surface loop on the design scaffold. The design scaffold's surface is then redesigned with backbone flexibility to create a new binding partner for the target. Careful choice of a scaffold will bring experimentally desirable characteristics into the new complex. The use of an anchor both expedites the design process and ensures that binding proceeds against a known location on the target. The use of surface loops on the scaffold allows for flexible-backbone redesign to properly search conformational space.This protocol was implemented within the Rosetta3 software suite. To demonstrate and evaluate this protocol, we have developed a benchmarking set of structures from the PDB with loop-mediated interfaces. This protocol can recover the correct loop-mediated interface in 15 out of 16 tested structures, using only a single residue as an anchor

Four Distances between Pairs of Amino Acids Provide a Precise Description of their Interaction

The three-dimensional structures of proteins are stabilized by the interactions between amino acid residues. Here we report a method where four distances are calculated between any two side chains to provide an exact spatial definition of their bonds. The data were binned into a four-dimensional grid and compared to a random model, from which the preference for specific four-distances was calculated. A clear relation between the quality of the experimental data and the tightness of the distance distribution was observed, with crystal structure data providing far tighter distance distributions than NMR data. Since the four-distance data have higher information content than classical bond descriptions, we were able to identify many unique inter-residue features not found previously in proteins. For example, we found that the side chains of Arg, Glu, Val and Leu are not symmetrical in respect to the interactions of their head groups. The described method may be developed into a function, which computationally models accurately protein structures