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  • Chemistry  (5)
  • AOT reverse micelle  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    FEBS Letters 178 (1984), S. 39-43 
    ISSN: 0014-5793
    Keywords: AOT reverse micelle ; Met-enkephalin ; NMR ; SDS micelle ; Shift reagent
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1075-2617
    Keywords: FMDV ; structure ; NMR spectrocopy ; NEO constraints ; RGD (Arg-Gly-Asp) ; Chemistry ; Biochemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The solution structure of a 20 amino acid long peptide corresponding to the region 141-160 of the envelope protein Vp1 from foot-and-mouth disease virus (FMDV) serotype A, variant A, has been determined by a combination of NMR experiments and computer calculations. The peptide contains both the immunodominant epitope as well as the sequence (RGD) used by the virus to bind the cell receptor in the initial stages of infection. These two sites have been shown to partially overlap.One hundred and thirty-five NMR distance constraints were used to obtain a set of 11 structures by distance geometry, minimization and molecular dynamics simulations. These structures were divided into two homogeneous families based upon backbone superimposition. The first and most populated family was characterized by a backbone RMS of 1.5±0.4 Å, the second by a backbone RMS of 0.8±0.2 Å. The two families had similar structural features and differed mainly in the backbone angles of G149. In the larger of the two families these angles favoured the formation of a loop comprising residues 147 to 152 and stabilized by a H-bond between the NH of D147 and the CO of A152. In the second family, where this bond was absent, the peptide adopted in this region the shape of an irregular helix. The C-terminal half of the peptide (152-159) was similar in both families and largely helical. Similar structural features were also found within the VRGDS sequence (144-148) which was assigned to a β-turn type IV. The features of the two families of structures were found to be different from those of the recently published X-ray structure of the antigenic loop of a chemically modified form of FMDV. Proposals accounting for these differences are provided which take into account the dual activity of the 141-160 sequence (i.e. antibody binding and cell invasion through receptor binding).
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1075-2617
    Keywords: FMDV ; NMR spectrocopy ; RGD (Arg-Gly-Asp) ; NEO constraints ; structure-activity correlation ; Chemistry ; Biochemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The solution structure of a peptide corresponding to the VP1 region 141-160 of foot-and-mouth disease virus (FMDV) serotype A variant USA has been studied by NMR and computer calculations and compared with the results from a study on a highly homologous peptide deriving from serotype A, variant A. The two peptides differ in their serological behaviour and contain the immunodominant epitope of the virus which partly overlaps with its receptor binding region. Distance constraints, derived both from 2D and 3D homonuclear NMR and 2D-heteronuclear NMR experiments, were combined with DG calculations to yield 50 structures. After refinement through EM and restrained molecular dynamics simulations the selected structures shared several general features. In particular the 151-158 region was a helix in all cases while a large loop similar to that found in peptide A but comprising less residues and stabilized by an H-bond between the side chains of D147 and S150 was found in the majority of structures. A further loop, common to all structures, was identified around the RGD sequence (145-147). This was different from that found in the corresponding region of peptide A as were the conformations of the individual residues within the RGDX sequence.The different structural features shown by the two peptides were rationalized in terms of the S148 (peptide A) to F148 (peptide USA) mutation. The second mutation, that at position 153 (L in A, P in USA) did not appear to affect the structure of the peptide significantly although the different dimensions of the loop in the central region and the type of H-bond stabilizing it could be potentially ascribed to this second mutation.All criteria used pointed to different structural features for the two peptides consistent with their serological behaviour.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Chichester : Wiley-Blackwell
    Organic Magnetic Resonance 9 (1977), S. 218-223 
    ISSN: 0030-4921
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The conformations of dihydrolysergamides and 10-methoxydihydrolysergamides have been inferred from the study of the chemical shifts of the amide hydrogens and their temperature dependence. The 13C chemical shifts have been shown to be sensitive to conformational changes of the piperidine ring. The results indicate that the conformation of the latter depends both on the substituent in position 10 and on the solvent.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Chichester : Wiley-Blackwell
    Organic Magnetic Resonance 4 (1972), S. 585-589 
    ISSN: 0030-4921
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Proton and carbon-13 spectra of benzyl compounds of the general formula (C6H5CH2)nX with a large variety of X substituents have been measured. While a linear relationship between the CH2 chemical shift and the substituent electronegativity was found both for 1H and 13C, large deviations from linearity were observed for transition metals such as titanium and zirconium. These later results are correlated with the X-ray studies of the latter compounds.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Chichester : Wiley-Blackwell
    Organic Magnetic Resonance 33 (1995), S. 586-591 
    ISSN: 0749-1581
    Keywords: 1H NMR ; amphipathic structure ; diphenylhydantoin derivatives ; anticonvulsants ; antidepressant ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The solution conformations of 1-benzyl-5,5-diphenyl-2,4-dioxo-3-imidazolidineacetic acid (AC) and 3-(2,4-dichlorobenzyl)-5,5-diphenyl-2,4-dioxo-1-imidazolidine acetic acid (AD) were studied by proton and carbon NMR spectroscopy. The two drugs have different pharmacological activities, AC having anticonvulsant and AD having antidepressant but no anticonvulsant properties. The relative orientations of the hydantoin ring substituents were investigated and are discussed in terms of amphipathic distribution of polar and apolar domains.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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