[en] The ¹H-NMR spectrum of MeSiCp determined at various temperatures is reported and discussed in terms of metallotropic and phototropic rearrangements. (author)

[en] An overview is given of the possibilities of ³H NMR in the characterisation of ³H-labelled compounds. This technique gives information on the identity of the tritiated compounds, the position of the tritium, the distribution of the label and even the radiochemical purity of the labelled products. (author)

[en] Brief item

No abstract available

[en] Functional interaction between Drosophila orphan receptor FTZ-F1 (NR5A3) and a segmentation gene product fushi tarazu (FTZ) is crucial for regulating genes related to define the identities of alternate segmental regions in the Drosophila embryo. FTZ binding to the ligand-binding domain (LBD) of FTZ-F1 is of essence in activating its transcription process. We determined solution structures of the cofactor peptide (FTZ^PEP) derived from FTZ by NMR spectroscopy. The cofactor peptide showed a nascent helical conformation in aqueous solution, however, the helicity was increased in the presence of TFE. Furthermore, FTZ^PEP formed α- helical conformation upon FTZ-F1 binding, which provides a receptor bound structure of FTZ^PEP. The solution structure of FTZ^PEP in the presence of FTZ-F1 displays a long stretch of the α-helix with a bend in the middle of helix

[en] Published in summary form only

[en] Tritium nmr spectroscopy of specifically tritiated tosylchymotrypsin has been used to examine the properties of the tosyl group in this protein. The unavoidable presence of several tritiated isotopomers complicates analysis of experiments and extensive computer simulations of relaxation behavior of tritiated species present were used in conjunction with models developed from crystallographic results to interpret the observations made. These analyses suggest that the tosyl group of tosylchymotrypsin at pH 4 is highly mobile in solution and occupies the location in the protein that is observed in the crystalline state only about 50% of the time. (author)

[en] Volume 10 of Annual Reports on NMR Spectroscopy consists of accounts covering three main areas of molecular science: NMR of living systems is covered for the first time in this series; various aspects of Boron NMR are dealt with in two, largely complementary chapters; the third area reported on is that of NMR studies of alkali anions in nonaqueous solvents

[en] A method for five-dimensional spectral reconstruction of non-uniformly sampled NMR data sets is proposed. It is derived from the previously published signal separation algorithm, with major alterations to avoid unfeasible processing of an entire five-dimensional spectrum. The proposed method allows credible reconstruction of spectra from as little as a few hundred data points and enables sensitive resonance detection in experiments with a high dynamic range of peak intensities. The efficiency of the method is demonstrated on two high-resolution spectra for rapid sequential assignment of intrinsically disordered proteins, namely 5D HN(CA)CONH and 5D (HACA)CON(CO)CONH.

[en] Functional interaction between Drosophila orphan receptor FTZ-F1 (NR5A3) and a segmentation gene product fushi tarazu (FTZ) is crucial for regulating genes related to define the identities of alternate segmental regions in the Drosophila embryo. FTZ binding to the ligand-binding domain (LBD) of FTZ-F1 is of essence in activating its transcription process. We determined solution structures of the cofactor peptide (FTZ^PEP) derived from FTZ by NMR spectroscopy. The cofactor peptide showed a nascent helical conformation in aqueous solution, however, the helicity was increased in the presence of TFE. Furthermore, FTZ^PEP formed α- helical conformation upon FTZ-F1 binding, which provides a receptor bound structure of FTZ^PEP. The solution structure of FTZ^PEP in the presence of FTZ-F1 displays a long stretch of the α-helix with a bend in the middle of helix