Slow turning reveals enormous quadrupolar interactions (STREAQI)

We introduce a new solid-state NMR method, which uses very slow sample rotation to visualize NMR spectra whose width exceeds feasible spectrometer bandwidths. It is based on the idea that if we reorient a tensor by a known angle about a known axis, the shifts in the NMR frequencies observed across the spectral width allow us to reconstruct the entire tensor. Called STREAQI (Slow Turning Reveals Enormous Anisotropic Quadrupolar Interactions), this method allows us to probe NMR nuclei that are intractable to current methods. To prove the concept and demonstrate its promise we have implemented the method for several 79Br containing samples with quadrupolar coupling constants in the range of 10-50 MHz.     

Evaluation of flush mounted hot-film sensors for skin friction reduction measurements in viscoelastic polymer solutions

The purpose of this investigation was to evaluate the performance of flush mounted hot-film sensors for mean wall shear stress measurement in turbulent flows of dilute drag reducing polymer solution. A series of pipe flow expriments were conducted over a range of Reynolds numbers and polymer solution concentrations to compare the level of skin friction drag reduction measured by hot-film sensors with values calculated from pipe pressure drop. It is shown that water calibrated hot-film sensors consistently underestimate the wall shear stress suggesting that Reynolds analogy is not valid in dilute polymer solutions. The Newtonian form of the relationship between the wall shear stress and the heat transfer remains valid in dilute polymer solutions. However, multiplicative and additive factors in the relationship are shown to increase linearly with the logarithm of the polymer concentration.     

A fluorescence technique for measurement of slot injected fluid concentration profiles in a turbulent boundary layer

A technique for measuring near instantaneous concentration profiles of a fluid injected through a narrow inclined slot at the wall into a high unit Reynolds number flat plate turbulent boundary layer is discussed. The concentration profiles are determined by measuring the light intensity emitted from a fluorescent dye, premixed into the injectant flow, as the injectant convects through an excitation laser beam. The fluorescence intensity is quantified by an electronically shuttered single stage microchannel plate image intensifier coupled to a linear photodiode array. This instrumentation provided the high spatial and temporal resolution required for these boundary layer concentration profile measurements. The laser induced fluorescence technique is being used to study the diffusion of injected polymer solutions away from the near wall region of the boundary layer where these solutions are effective in reducing drag. The diffusion of slot injected water has also been examined and the present results are in excellent agreement with previous studies.     

Mechanism for CuPt-type ordering in mixed III–V epitaxial layers

A model is proposed to rationalize the occurence of CuPt-type ordering in mixed III–V epitaxial layers grown on (001) substrates. It is invoked that 2× surface reconstruction occuring on group V terminated (001) surfaces produces dilated and compressed regions in sub-surface layers. The presence of these regions biases the occupation of certain sites during the growth of a layer consisting of atoms differing in their tetrahedral radii. By assuming that the reconstruction always occurs at the growing surface, it is possible to explain the evolution of CuPt-type ordering in epitaxial layers. Also, based on the model, experimental observations pertaining to the influence of growth conditions, surface misorientation and steps on ordering can be rationalized.     

Estimating protein-ligand binding affinity using high-throughput screening by NMR

Many of today's drug discovery programs use high-throughput screening methods that rely on quick evaluations of protein activity to rank potential chemical leads. By monitoring biologically relevant protein-ligand interactions, NMR can provide a means to validate these discovery leads and to optimize the drug discovery process. NMR-based screens typically use a change in chemical shift or line width to detect a protein-ligand interaction. However, the relatively low throughput of current NMR screens and their high demand on sample requirements generally makes it impractical to collect complete binding curves to measure the affinity for each compound in a large and diverse chemical library. As a result, NMR ligand screens are typically limited to identifying candidates that bind to a protein and do not give any estimate of the binding affinity. To address this issue, a methodology has been developed to rank binding affinities for ligands based on NMR screens that use 1D (1)H NMR line-broadening experiments. This method was demonstrated by using it to estimate the dissociation equilibrium constants for twelve ligands with the protein human serum albumin (HSA). The results were found to give good agreement with previous affinities that have been reported for these same ligands with HSA.