Monolayer transition-metal dichalcogenides (TMDs) have the potential to become efficient optical-gain materials for low-energy-consumption nanolasers with the smallest gain media because of strong excitonic emission. However, until now TMD-based lasing has been realized only at low temperatures. Here we demonstrate for the first time a room-temperature laser operation in the infrared region from a monolayer of molybdenum ditelluride on a silicon photonic-crystal cavity. The observation is enabled by the unique combination of a TMD monolayer with an emission wavelength transparent to silicon, and a high-Q cavity of the silicon nanobeam. The laser is pumped by a continuous-wave excitation, with a threshold density of 6.6 W cm. Its linewidth is as narrow as 0.202 nm with a corresponding Q of 5,603, the largest value reported for a TMD laser. This demonstration establishes TMDs as practical materials for integrated TMD-silicon nanolasers suitable for silicon-based nanophotonic applications in silicon-transparent wavelengths.

We have used ab initio quantum chemical techniques to compute the (13)C(alpha) and (13)C(beta) shielding surfaces for the 14 amino acids not previously investigated (R. H. Havlin et al., J. Am. Chem. Soc. 1997, 119, 11951-11958) in their most popular conformations. The spans (Omega = sigma(33) - sigma(11)) of all the tensors reported here are large ( approximately 34 ppm) and there are only very minor differences between helical and sheet residues. This is in contrast to the previous report in which Val, Ile and Thr were reported to have large ( approximately 12 ppm) differences in Omega between helical and sheet geometries. Apparently, only the beta-branched (beta-disubstituted) amino acids have such large CSA span (Omega) differences; however, there are uniformly large differences in the solution-NMR-determined CSA (Deltasigma = sigma(orth) - sigma(par)) between helices and sheets in all amino acids considered. This effect is overwhelmingly due to a change in shielding tensor orientation. With the aid of such shielding tensor orientation information, we computed Deltasigma values for all of the amino acids in calmodulin/M13 and ubiquitin. For ubiquitin, we find only a 2.7 ppm rmsd between theory and experiment for Deltasigma over an approximately 45 ppm range, a 0.96 slope, and an R(2) = 0.94 value when using an average solution NMR structure. We also report C(beta) shielding tensor results for these same amino acids, which reflect the small isotropic chemical shift differences seen experimentally, together with similar C(beta) shielding tensor magnitudes and orientations. In addition, we describe the results of calculations of C(alpha), C(beta), C(gamma)1, C(gamma)2, and C(delta) shifts in the two isoleucine residues in bovine pancreatic trypsin inhibitor and the four isoleucines in a cytochrome c and demonstrate that the side chain chemical shifts are strongly influenced by chi(2) torsion angle effects. There is very good agreement between theory and experiment using either X-ray or average solution NMR structures. Overall, these results show that both C(alpha) backbone chemical shift anisotropy results as well as backbone and side chain (13)C isotropic shifts can now be predicted with good accuracy by using quantum chemical methods, which should facilitate solution structure determination/refinement using such shielding tensor surface information.

We have carried out a solid-state magic-angle sample-spinning (MAS) nuclear magnetic resonance (NMR) spectroscopic investigation of the (13)C(alpha) chemical shielding tensors of alanine, valine, and leucine residues in a series of crystalline peptides of known structure. For alanine and leucine, which are not branched at the beta-carbon, the experimental chemical shift anisotropy (CSA) spans (Omega) are large, about 30 ppm, independent of whether the residues adopt helical or sheet geometries, and are in generally good accord with Omega values calculated by using ab initio Hartree-Fock quantum chemical methods. The experimental Omegas for valine C(alpha) in two peptides (in sheet geometries) are also large and in good agreement with theoretical predictions. In contrast, the "CSAs" (Deltasigma) obtained from solution NMR data for alanine, valine, and leucine residues in proteins show major differences, with helical residues having Deltasigma values of approximately 6 ppm while sheet residues have Deltasigma approximately 27 ppm. The origins of these differences are shown to be due to the different definitions of the CSA. When defined in terms of the solution NMR CSA, the solid-state results also show small helical but large sheet CSA values. These results are of interest since they lead to the idea that only the beta-branched amino acids threonine, valine, and isoleucine can have small (static) tensor spans, Omega (in helical geometries), and that the small helical "CSAs" seen in solution NMR are overwhelmingly dominated by changes in tensor orientation, from sheet to helix. These results have important implications for solid-state NMR structural studies which utilize the CSA span, Omega, to differentiate between helical and sheet residues. Specifically, there will be only a small degree of spectral editing possible in solid proteins since the spans, Omega, for the dominant nonbranched amino acids are quite similar. Editing on the basis of Omega will, however, be very effective for many Thr, Val, and Ileu residues, which frequently have small ( approximately 15-20 ppm) helical CSA (Omega) spans.

This paper will present a complete formulation of the optimal control problem for atmospheric ascent of rocket powered launch vehicles subject to usual load constraints and final conditionconstraints. We shall demonstrate that the classical finite difference method for two-point-boundaxy-value-problems (TPBVP) is suited for solving the ascent trajectory optimization problem in real time, therefore closed-loop optimal endoatmospheric ascent guidance becomes feasible. Numerical simulations with a the vehicle data of a reusable launch vehicle will be provided. AscentGuidance Problem FormulationThe equations of motion of the RLV in an inertial coordinate system can be expressed aswhere r and V are inertial position and velocity vectors; g the gravitational acceleration;T the thrust magnitude; A and N are aerodynamic axial and normal forces, respectively; lb the unit vector defining the RLV body longitudinal axis; m is the mass of the RLV. The magnitudes of the aerodynamic forces and thrust are modeled bywhere p is the atmospheric density, and Vr is the magnitude of the Earth-relative velocity V, = V -_E X r with _s being the Earth angular rotation rate vector.

We report the first solid-state NMR, crystallographic, and quantum chemical investigation of the origins of the 13C NMR chemical shifts of the imidazole group in histidine-containing dipeptides. The chemical shift ranges for Cgamma and Cdelta2 seen in eight crystalline dipeptides were very large (12.7-13.8 ppm); the shifts were highly correlated (R2= 0.90) and were dominated by ring tautomer effects and intermolecular interactions. A similar correlation was found in proteins, but only for buried residues. The imidazole 13C NMR chemical shifts were predicted with an overall rms error of 1.6-1.9 ppm over a 26 ppm range, by using quantum chemical methods. Incorporation of hydrogen bond partner molecules was found to be essential in order to reproduce the chemical shifts seen experimentally. Using AIM (atoms in molecules) theory we found that essentially all interactions were of a closed shell nature and the hydrogen bond critical point properties were highly correlated with the N...H...O (average R2= 0.93) and Nepsilon2...H...N (average R2= 0.98) hydrogen bond lengths. For Cepsilon1, the 13C chemical shifts were also highly correlated with each of these properties (at the Nepsilon2 site), indicating the dominance of intermolecular interactions for Cepsilon1. These results open up the way to analyzing 13C NMR chemical shifts, tautomer states (from Cdelta2, Cepsilon1 shifts), and hydrogen bond properties (from Cepsilon1 shifts) of histidine residue in proteins and should be applicable to imidazole-containing drug molecules bound to proteins, as well.

By using density functional theory it is demonstrated that the long-range 19 F-19 F J-couplings ( >3 J) seen in small organic molecules can be calculated with good accuracy using small molecule fragments and in some cases complete molecules. The results reproduce the exponential distance dependence of J seen experimentally, demonstrate the dominance of the Fermi contact interaction, and rule out any significant covalent or through-bond contributions to J in these systems. The calculations also verify an experimentally observed 19 F-19 F J-coupling seen between two [6-F]Trp residues in the protein dihydrofolate reductase (for d ) 2.98 Å), where there is clearly no covalent bonding between the two 19 F sites. The results also clarify the abnormally small J-couplings seen previously in phenanthrenes and cyclohexenes, which are shown by ab initio and molecular mechanics geometry optimizations to be due to conversion of the supposedly planar structures to more distorted but less sterically hindered structures. These distortions increase the F-F distance and thereby reduce J FF . The lack of any appreciable covalent bonding between the 19 F atoms in both the protein and the model systems, but the presence of significant J-couplings, emphasizes that all that is required is Fermi contact, and the close spatial proximity of atoms. This result is of considerable current interest in the context of (long range/through-space) hydrogen bond J-couplings in macromolecules.

We have used density functional theory methods to investigate the solid-state "magic-angle" spinning (MAS) NMR and single-crystal NMR/ENDOR spectra of paramagnetic organometallic complexes and metalloporphyrins. The solid-state MAS NMR chemical shifts (including both diamagnetic and hyperfine contributions) are predicted with a slope of 1.007 and an R2 = 0.967, corresponding to a 28 ppm (or 6.3%) error over the entire 442 ppm range. Single-crystal ENDOR hyperfine values, including both isotropic Fermi contact and dipolar couplings, are predicted with a slope of 1.009 and an R2 = 0.998, corresponding to a 0.93 MHz (or 1.2%) error over the entire 78.37 MHz range. In addition, single-crystal NMR shifts (including both hyperfine terms) are predicted with an R2 = 0.961. The ability to compute solid-state MAS NMR and single-crystal NMR/ENDOR data should facilitate the use of these techniques in investigating paramagnetic metal complexes and should be of particular use in studying paramagnetic metalloproteins, where structures are less accurately known.

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