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  • 1
    Electronic Resource
    Electronic Resource
    Photocatalyzed Oxidation of Cyclohexene and Cyclooctene with (nBu4N)4W10O32 and (nBu4N)4W10O32/FeIII[meso-Tetrakis(2,6-dichlorophenyl)porphyrin] in Homogeneous and Heterogeneous Systems (2000)
    Weinheim : Wiley-Blackwell
    Berichte der deutschen chemischen Gesellschaft 2000 (2000), S. 91-96 
    Details
    ISSN: 1434-1948
    Keywords: Photocatalysis ; Polyoxotungstates ; Catalytic oxidations ; Iron porphyrins ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Photoexcitation of (nBu4N)4W10O32 is a suitable mean of oxidizing cyclohexene and cyclooctene with O2 at room temperature and pressure. This process can be carried out in homogeneous solution as well as using the decatungstate in a dispersed form after its heterogenisation on silica. Cyclohexene and cyclooctene are mainly oxidized to the corresponding hydroperoxides as a consequence of primary photoprocesses which lead to the formation of allylic radicals. The presence of the FeIII[meso-tetrakis(2,6-dichlorophenyl)porphyrin] chloride as cocatalyst strongly affects the photocatalytic properties of (nBu4N)4W10O32, playing a key role in the allylic-hydroperoxide dependent oxidation of the cycloalkenes. In the photooxidation of cyclohexene, the porphyrin increases the photocatalytic efficiency of the decatungstate in terms of total turnover number and catalyses the decomposition of cyclohexenyl hydroperoxide with the selective formation of cyclohex-2-en-1-ol. On the other hand, its presence during the photoinduced oxidation of cyclooctene favours the formation of cyclooctene epoxide by addition of ROO· and RO· radicals to the double bond. In the case of cyclooctene, the heterogenisation of the decatungstate on the solid support also affects the chemoselectivity of the photocatalytic process in the absence of the iron porphyrin complex.
    Additional Material: 1 Ill.
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  • 2
    Electronic Resource
    Electronic Resource
    Selection of a chemically defined medium for submerged cultivation of Streptomyces aureofaciens with high extracellular caseinolytic activity (1977)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 19 (1977), S. 1863-1884 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A chemically defined medium was developed for the submerged cultivation of Streptomyces aureofaciens with a high secretion of caseinolytic activity. The medium composition is: 40 g/liter maltose; 1.640 g/liter L-leucine (0.0125M); 1.765 g/liter L-lysine (0.0125M); 6.976 g/liter K2HPO4(0.04M); 4 g/liter CaCO3; 0.2 g/liter MgSO4·7H2O; 0.01 g/liter ZnSO4·7H2O; 0.01 g/liter FeSO4·7H2O; 0.01 g/liter. MnSO4·H2O, and 0.005 g/liter CoSO4·7H2O. Quantitative correlations were established between the concentrations of nutrients in the medium and the secretion of proteolytic activity. In this medium the secretion of proteolytic activity parallels growth, reaching a maximum after 70 hr at 30°C in shaker cultures. The secretion appears to be an active process and to require aerobic conditions.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260191210
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  • 3
    Electronic Resource
    Electronic Resource
    Fractionation of the proteolytic and amylolytic complex enzyme system of Streptomyces aureofaciens and some properties of fractions (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 21 (1979), S. 915-938 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The Streptomyces aureofaciens extracellular proteolytic system was split into four fractions by carboxymethylcellulose (CMC) column chromatography giving three purely caseinolytic fractions and one fraction active toward both starch and casein. The first caseinolytic and amylolytic fraction was further fractionated by DEAE-Sephadex A-50 chromatography into one purely amylolytic fraction and another showing both activities, was refractioned into four new fractions by DEAE-cellulose chromatography. These fractions were found to be heterogeneous by polyacrylamide gel electrophoresis, three of them acted on both starch and casein and a fourth was only caseinolytic. The second CMC fraction was further purified by CMC rechromatography to an homogeneous fraction that hydrolyzes carboxypeptidase A(EC 3.4.2.1) synthetic substrates and solubilizes elastin. It had only one polypeptide chain with a molecular weight of about 28000 daltons, a high thermal stability in the presence of calcium ions, a pH optimum of about 6.8, and a maximal caseinolytic activity at about 50°C.
    Additional Material: 14 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260210602
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  • 4
    Electronic Resource
    Electronic Resource
    True cosolvency. Acetone/diethylether/polystyrene (1973)
    New York : Wiley-Blackwell
    Die Makromolekulare Chemie 173 (1973), S. 241-245 
    Details
    ISSN: 0025-116X
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/macp.1973.021730118
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  • 5
    Electronic Resource
    Electronic Resource
    The Solution Conformational Features of Two Highly Homologous Antigenic Peptides of Foot-and-mouth Disease Virus Serotype A, Variants A and USA, Correlate with their Serological Properties (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 2 (1996), S. 91-105 
    Details
    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
    URL: http://dx.doi.org/10.1002/psc.50
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  • 6
    Electronic Resource
    Electronic Resource
    The design of a specific ligand of HIV gp120 (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 3 (1997), S. 383-390 
    Details
    ISSN: 1075-2617
    Keywords: CD4 ; gp120 ; NMR ; structure ; peptides ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The crystal structure of CD4 suggested that the C/G38 and C/L44 replacements with the consequent cystine bridge formation are compatible with the native structure of that molecular moiety. As the NQGSF sequence, corresponding to the 39-43 fragment of human CD4 protein, was found to be involved in the HIV gp120 interaction, it has been synthesized in a cyclic form by adding two cysteine residues at the amino and carboxy termini. 1H-NMR studies show that the predominant solution conformation of cyclo-[CNQGSFC] is a type II β-turn centred on the NQGS segment. Structural and dynamic properties of the peptide are also analysed in relation to the in vitro activity. © 1997 European Peptide Society and John Wiley & Sons, Ltd.J. Pep. Sci. 3: 383-390No. of Figures: 7. No. of Tables: 1. No. of References: 33.
    Additional Material: 7 Ill.
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  • 7
    Electronic Resource
    Electronic Resource
    The Solution Structure of the Immunodominant and Cell Receptor Binding Regions of Foot-and-mouth Disease Virus Serotype A, Variant A (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 2 (1996), S. 75-90 
    Details
    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
    URL: http://dx.doi.org/10.1002/psc.49
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  • 8
    Electronic Resource
    Electronic Resource
    1H- and natural abundance 15N-nmr studies of a derivative of a rabies glycoprotein fragmentDedicated to the memory of Antonio De Marco. (1991)
    New York : Wiley-Blackwell
    Biopolymers 31 (1991), S. 713-723 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Using a combination of one- and two-dimensional methods, 1H- and 15N-nmr spectroscopy has been employed to perform the complete assignment and the structural determination of the immunogenic undecapeptide CTTTNSRGTTT in DMSO solution. Nuclear Over-hauser enhancement spectroscopy experiments indicated the presence of secondary structures, mainly turn-like structures, which only represent a family, albeit a dominant one, of an ensemble of conformations available to the peptide. Since reverse turns may play an important role as intermediates in protein folding, the experimental observations described here may link the immunological and theoretical approaches to protein folding.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360310616
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  • 9
    Electronic Resource
    Electronic Resource
    Probing protein structure by solvent perturbation of nmr spectra. II. Determination of surface and buried residues in homologous proteins (1993)
    New York : Wiley-Blackwell
    Biopolymers 33 (1993), S. 839-846 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The experimental assignment of most residues in a protein to the surface or interior is in principle possible without prior solution of a complete three-dimensional structure. The method described is based on nmr measurements that determine the amino acid composition of the surface of a protein [A. Petros, L. Mueller, and K. D. Kopple (1990) Biochemistry, Vol. 29, pp. 10041-10048; G. Esposito, A. M. Lesk, H. Molinari, A. Motta, N. Niccolai, and A. Pastore (1992) Journal of Molecular Biology, Vol. 224, pp. 659-670]. If these measurements are carried out on several homologous proteins of known sequence, it is possible to combine the results to determine, in most cases, which positions in the sequence contain exposed residues. © 1993 John Wiley & Sons, Inc.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360330512
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  • 10
    Electronic Resource
    Electronic Resource
    CD and NMR structural characterization of ceratotoxins, natural peptides with antimicrobial activity (1996)
    New York : Wiley-Blackwell
    Biopolymers 39 (1996), S. 653-664 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Antibacterial properties of the secretion from the female reproductive accessory glands of medfly Ceratitis capitata are mostly ascribed to the presence of two peptides, ceratotoxin A and B, which exhibit a strong activity against gram-positive and gram-negative bacterial strains, and show sequence and function homology with cecropins, melittin, and magainins.CD experiments performed in different solvents indicate the presence of a significant content of helical structures in organic solvent.Two-dimensional nmr results for ceratotoxin A in methanol show a helical behavior for the 8-25 region of the peptide. A Ramachandran classification of each residue for the structures obtained from distance geometry calculations lead to the definition of four structural families in which the central segment 10-19 is always helical and differences refer to residues 8-9 and 19-23.A sequence analysis of the two ceratotoxins and a systematic search on the protein data bank revealed the occurrence of a KX-hydrophobic-hydrophobic-P motif that seems to be important for helix stabilization. © 1996 John Wiley & Sons, Inc.
    Additional Material: 6 Ill.
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