A comparative fMRI study: T2*-weighted imaging versus R2* mapping.

Functional magnetic resonance imaging experiments were performed in human motor cortex at 1.5 T by sampling two successive gradient recalled echo images in a single shot. Several aspects of brain mapping methods based on T2*-weighted imaging and R2* mapping were quantitatively compared. These include the detected activation volume, functional contrast (FC), signal-to-noise ratio (SNR), and contrast-to-noise ratio (CNR). Studies based on the R2* mapping method have the following potential advantages: maximum functional contrast, less dependent on TE; and reduced inflow effects. R2* mapping produced the highest functional contrast, but not the largest activation volume due to the reduced signal-to-noise ratio and inflow effects. The sensitivity for activation detection is significantly correlated with the contrast-to-noise ratio, which is determined by both the SNR and FC.

Current awareness in NMR in biomedicine.

In order to keep subscribers up-to-date with the latest developments in their field, John Wiley & Sons are providing a current awareness service in each issue of the journal. The bibliography contains newly published material in the field of NMR in biomedicine. Each bibliography is divided into 9 sections: 1 Books, Reviews ' Symposia; 2 General; 3 Technology; 4 Brain and Nerves; 5 Neuropathology; 6 Cancer; 7 Cardiac, Vascular and Respiratory Systems; 8 Liver, Kidney and Other Organs; 9 Muscle and Orthopaedic. Within each section, articles are listed in alphabetical order with respect to author. If, in the preceding period, no publications are located relevant to any one of these headings, that section will be omitted.

An image registration strategy for multi-echo fMRI.

Functional magnetic resonance imaging (fMRI) based on multiple-echo T(2)* mapping has attracted much attention recently. The contrasts in the parametric T(2)* maps are usually too low to allow direct image registration. In this study, an image registration strategy has been proposed for single-shot multi-echo data sets acquired for dynamic T(2)* mapping. We performed image registration of the T(2)*-weighted images before the calculation of the T(2)* parameter maps using two different strategies. One is to perform separate image registration on each echo and the other is to use the same motion correction parameters extracted from the second echo for all the data. Both strategies increase the number of activated voxels and reduce the effective noise level. The results also indicate that, for a single-shot dual-echo image data set, it is slightly preferable to use the second echo for direct image registration and then apply the same motion correction parameters to the first echo images. J. Magn. Reson Imaging 1999;10:154-158.

Conformational analysis of galanin using end to end distance distribution observed by Förster resonance energy transfer.

The structural dynamics of the flexible neuropeptide galanin in solution were studied by Förster resonance energy transfer measurements at different temperatures by time-resolved fluorescence spectroscopy to determine its conformational heterogeneity. Endogenous tryptophan at position 2 acted as the fluorescent donor and the non fluorescent acceptor dinitrophenyl or the fluorescent acceptor dansyl were selectively attached to lysine 25 in porcine galanin. The coexistence of different structures of the neuropeptide galanin in trifluoroethanol solution was revealed by the model independent analysis of the distribution of relaxation times from the time-resolved resonance energy transfer data. Multiple conformational states are reflected by distinct end-to-end distance populations. The conformations differ in mean donor-acceptor distance by about 15, and are consistent with the extended and folded backbone conformations of two alpha-helical regions separated by a flexible hinge. The effect that the labelling of galanin has on binding to the receptor was also evaluated. DNP-galanin showed the same high affinity to galanin receptors as unlabelled galanin, whereas DNS-galanin had significantly reduced affinity.

A 1H NMR study of the solution conformation of the neuropeptide galanin.

The conformations of the neuropeptide galanin in water and trifluoroethanol solutions have been examined by 1H NMR spectroscopy. Analysis of two-dimensional NMR experiments enabled the assignment of virtually all the 1H resonances of galanin in trifluoroethanol solution and many of the 1H resonances in aqueous solution. Interpretation of the NMR data in structural terms suggests that in trifluoroethanol galanin is predominantly helical while in water it does not adopt a fixed conformation.