System model for studying fibre grating dispersion compensators

A complete optical system model has been developed and used to assess chirped fibre Bragg grating dispersion compensators. Gratings suitable for dispersion compensation in both laser based and modulator based optical communications systems have been modelled. A grating 10 cm in length has been shown to permit virtually dispersion free transmission over 425 km, when used in an externally modulated system. Long haul dispersion compensation using several 2 cm gratings spaced at intervals along the fibre is also modelled, illustrating viable 10Gbit/s transmission over a distance in excess of 168 km.

Computational mechanisms of sensorimotor control.

In order to generate skilled and efficient actions, the motor system must find solutions to several problems inherent in sensorimotor control, including nonlinearity, nonstationarity, delays, redundancy, uncertainty, and noise. We review these problems and five computational mechanisms that the brain may use to limit their deleterious effects: optimal feedback control, impedance control, predictive control, Bayesian decision theory, and sensorimotor learning. Together, these computational mechanisms allow skilled and fluent sensorimotor behavior.

Eigenmodes of lined flow ducts with rigid splices

This paper presents an analytic expression for the acoustic eigenmodes of a cylindrical lined duct with rigid axially running splices in the presence of flow. The cylindrical duct is considered to be uniformly lined except for two symmetrically positioned axially running rigid liner splices. An exact analytic expression for the acoustic pressure eigenmodes is given in terms of an azimuthal Fourier sum, with the Fourier coefficients given by a recurrence relation. Since this expression is derived using a Greens function method, the completeness of the expansion is guaranteed. A numerical procedure is described for solving this recurrence relation, which is found to converge exponentially with respect to number of Fourier terms used and is in practice quick to compute; this is then used to give several numerical examples for both uniform and sheared mean flow. An asymptotic expression is derived to directly calculate the pressure eigenmodes for thin splices. This asymptotic expression is shown to be quantitatively accurate for ducts with very thin splices of less than 1 % unlined area and qualitatively helpful for thicker splices of the order of 6 % unlined area. A thin splice is in some cases shown to increase the damping of certain acoustic modes. The influences of thin splices and thin boundary layers are compared and found to be of comparable magnitude for the parameters considered. Trapped modes at the splices are also identified and investigated. © 2011 Cambridge University Press.

Nanobodies raised against monomeric α-synuclein distinguish between fibrils at different maturation stages.

Nanobodies are single-domain fragments of camelid antibodies that are emerging as versatile tools in biotechnology. We describe here the interactions of a specific nanobody, NbSyn87, with the monomeric and fibrillar forms of α-synuclein (αSyn), a 140-residue protein whose aggregation is associated with Parkinson's disease. We have characterized these interactions using a range of biophysical techniques, including nuclear magnetic resonance and circular dichroism spectroscopy, isothermal titration calorimetry and quartz crystal microbalance measurements. In addition, we have compared the results with those that we have reported previously for a different nanobody, NbSyn2, also raised against monomeric αSyn. This comparison indicates that NbSyn87 and NbSyn2 bind with nanomolar affinity to distinctive epitopes within the C-terminal domain of soluble αSyn, comprising approximately amino acids 118-131 and 137-140, respectively. The calorimetric and quartz crystal microbalance data indicate that the epitopes of both nanobodies are still accessible when αSyn converts into its fibrillar structure. The apparent affinities and other thermodynamic parameters defining the binding between the nanobody and the fibrils, however, vary significantly with the length of time that the process of fibril formation has been allowed to progress and with the conditions under which formation occurs, indicating that the environment of the C-terminal domain of αSyn changes as fibril assembly takes place. These results demonstrate that nanobodies are able to target forms of potentially pathogenic aggregates that differ from each other in relatively minor details of their structure, such as those associated with fibril maturation.

Nanobodies raised against monomeric α-synuclein distinguish between fibrils at different maturation stages

Nanobodies are single-domain fragments of camelid antibodies that are emerging as versatile tools in biotechnology. We describe here the interactions of a specific nanobody, NbSyn87, with the monomeric and fibrillar forms of α-synuclein (αSyn), a 140-residue protein whose aggregation is associated with Parkinson's disease. We have characterized these interactions using a range of biophysical techniques, including nuclear magnetic resonance and circular dichroism spectroscopy, isothermal titration calorimetry and quartz crystal microbalance measurements. In addition, we have compared the results with those that we have reported previously for a different nanobody, NbSyn2, also raised against monomeric αSyn. This comparison indicates that NbSyn87 and NbSyn2 bind with nanomolar affinity to distinctive epitopes within the C-terminal domain of soluble αSyn, comprising approximately amino acids 118-131 and 137-140, respectively. The calorimetric and quartz crystal microbalance data indicate that the epitopes of both nanobodies are still accessible when αSyn converts into its fibrillar structure. The apparent affinities and other thermodynamic parameters defining the binding between the nanobody and the fibrils, however, vary significantly with the length of time that the process of fibril formation has been allowed to progress and with the conditions under which formation occurs, indicating that the environment of the C-terminal domain of αSyn changes as fibril assembly takes place. These results demonstrate that nanobodies are able to target forms of potentially pathogenic aggregates that differ from each other in relatively minor details of their structure, such as those associated with fibril maturation. © 2013 Elsevier Ltd.