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  • Artikel: DFG Deutsche Nationallizenzen  (105)
  • Biochemistry and Biotechnology  (82)
  • Organic Chemistry  (23)
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  • Artikel: DFG Deutsche Nationallizenzen  (105)
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Erscheinungszeitraum
  • 1
    Digitale Medien
    Digitale Medien
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 14 (1972), S. 915-938 
    ISSN: 0006-3592
    Schlagwort(e): Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: The integro-differential growth model of Eakman, Fredriekson, and Tsuehiya has been employed to fit cell size distribution data for Schizosaccharomyces pombe grown in a chemostat under severe product inhibition by ethanol. The distributions were obtained with a Coulter aperture and an electronic system patterned after that of Harvey and Marr. Four parameters - mean cell division size, cell division size standard deviation, daughter cell size standard deviation, and a growth rate coefficient - were calculated for models where the cell growth rate was inversely proportional to size, constant, and proportional to size. A fourth model, one where sigmoidal growth behavior was simulated by two linear growth segments, was also investigated. Linear and sigmoidal models fit the distribution data best. While the mean cell division size remained relatively constant at all growth rates, standard deviation of division size distribution increased with increasing holding times. Standard deviation of the daughter size distribution remained small at all dilution rates. Unlike previous findings with other organisms, the average cell size of Schizosaccharomyces pobme increased at low growth rates.
    Zusätzliches Material: 7 Ill.
    Materialart: Digitale Medien
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  • 2
    ISSN: 0018-019X
    Schlagwort(e): Chemistry ; Organic Chemistry
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: The temperature- and pressure-dependent equilibria for the addition of an extra N, N-dimethylforrnamide (DMF) or trimethylphosphate (TMP) ligand onto [Nd (DMF)8]3+- and [Nd(TMP)6]3+-species respectively have been measured by visible spectrophotometry. Complementary NMR. studies on other lanthanide ions show a gradual shift in preference for the lower coordination number across the lanthanide series.
    Zusätzliches Material: 2 Ill.
    Materialart: Digitale Medien
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  • 3
    ISSN: 0018-019X
    Schlagwort(e): Chemistry ; Organic Chemistry
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: Repetitive treatment of the biopolymer P(3-HB) (molecular weight 〉 105 Dalton, storage or s-P(3-HB)), with lithium hexamethyl disilazanid (LHMDS) at -70° in THF leads to a mixture of oligomers with increasingly sharp distribution around a 15-, 30-, and 45mer. Discrete fragments are also isolated when P(3-HB) is heated under reflux (89°) in neat Et3N. Linear oligo(3-HB) derivatives (3-7) containing up to 96 3-HB units are synthesized using an exponential segment-coupling strategy. These oligomers are used to calibrate size-exclusion chromatography columns for the analysis of oligo(3-HB) samples from the different sources. The linear oligo-(3-HB) derivatives also served as a model with respect to the physical properties of high molecular weight P(3-HB) and were investigated as such by transmission electron microscopy (TEM) and by small- and wide-angle X-ray scattering (SAXS and WAXS). The thicknesses of the lamellar crystallites (long periods) formed by the 8mer, 16mer, and 32mer, are ca. 26, 52, and 53 Å, respectively, indicating that the 32mer molecules are folded once, very tightly, into a ‘hair-pin’-type conformation. High-molecular-weight P(3-HB), which was crystallized in a similar way, also has a lamellar crystallite thickness of ca. 50-65 Å. Thus, the treatment of P(3-HB) with LHMDS at low temperature causes etching of the amorphous regions, an effect well known in polymer science for studying the regularity of chain folding. The ca. 50-Å packing within the tight folds of P(3-HB) is discussed in view of its possible function in ion transport through cell membranes.
    Zusätzliches Material: 10 Ill.
    Materialart: Digitale Medien
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  • 4
    ISSN: 0018-019X
    Schlagwort(e): Chemistry ; Organic Chemistry
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: Volumes of activation for the base hydrolysis of the dichromate anion have been measured at 298.2 K, using high-pressure stopped-flow spectrophotometry. The values of ΔV* (cm3 · mol-1), - 17.9 ± 0.6, - 19.2 ± 0.9, - 24.9 ± 0.9 and - 26.0 ± 0.7 for OH-, NH3, H2O and 2,6-lutidine, respectively, are consistent with an interchange mechanism with associative activation mode (Ia).
    Zusätzliches Material: 3 Ill.
    Materialart: Digitale Medien
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  • 5
    ISSN: 0018-019X
    Schlagwort(e): Chemistry ; Organic Chemistry
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: Dendritic iron porphyrins were synthesized as functional mimics of globular electron-transfer heme proteins. The cascade molecules 1 · Zn-3 Zn of first to third generation were obtained starting from the (meso-diarylporphyrin) zinc 6 · Zn which contains four carboxylate arms for attachment of the poly(ether-amide) dendritic branches by peptide-coupling methodology (Scheme 1). Generation 3 compound 3 · Zn with 108 methyl-carboxylate end groups has a molecular weight of 19054. D, and computer modeling suggests that its structure is globular and densely-packed, measuring ca. 4 nm in diameter and, therefore, similar in dimensions to the electron-transfer protein cytochrome-c. Starting from the generation 1 poly(carboxylic acid) 11 · Zn and the generation 2 analog 12 · Zn the dendritic ZnII porphyrins 4 · Zn and 5 · Zn, respectively, were obtained by esterification with triethyleneglycol monomethyl ether (Schemes 3 and 4). Demetallation followed by insertion of FeII and in situ oxidation afforded the water-soluble dendritic iron porphyrins 4 FeCl and 5 FeCl. The electrochemical behavior of esters 1 · Zn-3 · Zn in organic solvents changed smoothly with increasing dendritic generation (Table 1). Progressing from 1 · Zn to 3 · Zn in THF, the first porphyrin-centered oxidation and reduction potentials become more negative by 320 and 210mV, respectively. These changes were attributed to strong microenvironmental effects imposed on the electroactive core by the densely packed dendritic surroundings. The electrochemical properties of 4 · FeCl and 5 · FeCl were investigated by cyclic voltammetry in both CH2Cl2 and H2O (Tables 2 and 3). Progressing from 4 · FeCl to 5 · FeCl in CH2Cl2, the redox potential of the biologically relevant FeIII/FeII couple remained virtually unchanged, whereas in aqueous solution, 5 FeCl exhibited a potential 420 mV more positive than did 4 FeCl. The large difference between these potentials in H2O was attributed to differences in solvation of the core electrophore. Whereas the relatively open dendritic branches in 4 · Fecl do not impede access of bulk solvent to the central core, the densely packed dendritic superstructure of 5 · FeCl significantly reduces contact between the heme and external solvent. As a result, the more charged FeIII state is destabilized relative to FeII, and the redox potential is strongly shifted to a more positive value.
    Zusätzliches Material: 8 Ill.
    Materialart: Digitale Medien
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  • 6
    Digitale Medien
    Digitale Medien
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 56 (1997), S. 9-22 
    ISSN: 0006-3592
    Schlagwort(e): condensation reactions ; disaccharides ; equilibria ; glucoamylase ; kinetics ; monosaccharides ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Arabinose, fructose, galactose, myo-inositol, lyxose, mannose, ribose, and xylose were incubated individually and with glucose in the presence of Aspergillus niger glucoamylase at pH 4.5 and 45°C. Glucoamylase condenses galactose, glucose, and mannose individually into disaccharides. It also produces mixed disaccharides when each of the eight carbohydrates is incubated with glucose. Many products were identified by gas chromatography of the derivatized reaction mixtures followed by mass spectroscopy of the individual chromatographic peaks. Galacto-, gluco-, or mannopyranosyl rings appear to be present at the nonreducing ends of all the disaccharides produced. Molecules linked through primary hydroxyl groups have the highest equilibrium constants of all products formed, since these bonds are thermodynamically favored. However, glucoamylase is capable of forming bonds with many available hydroxyl groups, as previously demonstrated when it was incubated with glucose alone. Formation rates of different bonds linking different residues vary widely. These results demonstrate that glucoamylase has a wide selectivity toward residues it will condense into disaccharides and toward bonds it will form between them. © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 56: 9-22, 1997.
    Zusätzliches Material: 2 Ill.
    Materialart: Digitale Medien
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  • 7
    ISSN: 0887-3585
    Schlagwort(e): de novo design ; protein structure ; inverse folding ; genetic algorithms ; 1H NMR ; CD ; peptide ; protein folding ; methanol ; ethylene glycol ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Medizin
    Notizen: In response to the Paracelsus Challenge (Rose and Creamer, Proteins, 19:1-3, 1994), we present here the design, synthesis, and characterization of a helical protein, whose sequence is 50% identical to that of an all-β protein. The new sequence was derived by applying an inverse protein folding approach, in which the sequence was optimized to “fit” the new helical structure, but constrained to retain 50% of the original amino acid residues. The program utilizes a genetic algorithm to optimize the sequence, together with empirical potentials of mean force to evaluate the sequence-structure compatibility. Although the designed sequence has little ordered (secondary) structure in water, circular dichroism and nuclear magnetic resonance data show clear evidence for significant helical content in water/ethylene glycol and in water/methanol mixtures at low temperatures, as well as melting behavior indicative of cooperative folding. We believe that this represents a significant step toward meeting the Paracelsus Challenge.
    Zusätzliches Material: 5 Ill.
    Materialart: Digitale Medien
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  • 8
    Digitale Medien
    Digitale Medien
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 27 (1997), S. 235-248 
    ISSN: 0887-3585
    Schlagwort(e): acarviosinide ; active site ; docking ; glucoamylase ; molecular mechanics ; monosaccharides ; simulated annealing ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Medizin
    Notizen: Glucoamylase is an important industrial glucohydrolase with a large specificity range. To investigate its interaction with the monosaccharides D-glucose, D-mannose, and D-galactose and with the substrate analogues 1-deoxynojirimycin, D-glucono-1,5-lactone, and methyl αacarviosinide, MM3(92)-optimized structures were docked into its active site using AutoDock 2.1. The results were compared to structures of glucoamylase complexes obtained by protein crystallography. Charged forms of some substrate analogues were also docked to assess the degree of protonation possessed by glucoamylase inhibitors. Many forms of methyl αa-carviosinide were conformationally mapped by using MM3(92), characterizing the conformational pH dependence found for the acarbose family of glucosidase inhibitors. Their significant conformers, representing the most common states of the inhibitor, were used as initial structures for docking. This constitutes a new approach for the exploration of binding modes of carbohydrate chains. Docking results differ slightly from x-ray crystallographic data, the difference being of the order of the crystallographic error. The estimated energetic interactions, even though agreeing in some cases with experimental binding kinetics, are only qualitative due to the large approximations made by AudoDock force field. © 1997 Wiley-Liss, Inc.
    Zusätzliches Material: 4 Ill.
    Materialart: Digitale Medien
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  • 9
    ISSN: 0887-3585
    Schlagwort(e): X-ray crystallography ; antibody domain ; recombinant DNA ; binding affinity ; antigen-antibody complex ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Medizin
    Notizen: The variable heavy (VH) and variable light (VL) genes of NC10, a monoclonal antibody with specificity toward N9 neuraminidase (NA), were cloned and sequenced. A single chain Fv (scFv) fragment of NC10, consisting of VH and VL domains joined by a peptide linker, was designed, constructed and expressed in the E. coli expression vector pPOW. The N-terminal secretion signal PelB directed the synthesized protein into the periplasm where it was associated with the insoluble membrane fraction. An octapeptide (FLAG) tail was fused to the C-terminus of the single chain Fv to aid in its detection and remained intact throughout the protein purification process. NC10 scFv was purified by solubilization of the E. coli membrane fraction with guanidinium hydrochloride followed by column chromatography. The purified NC10 scFv showed binding affinity for its antigen, NA, 2-fold lower than that of the parent Fab. The complex between NA and the scFv has been crystallized by the vapor diffusion method. The crystals are tetragonal, space group P4212, with unit cell dimensions a = b = 141 Å, c = 218 Å. © 1993 Wiley-Liss, Inc.
    Zusätzliches Material: 4 Ill.
    Materialart: Digitale Medien
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  • 10
    Digitale Medien
    Digitale Medien
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 29 (1997), S. 123-128 
    ISSN: 0887-3585
    Schlagwort(e): protein structure prediction ; hidden Markov models ; fold recognition ; secondary structure ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Medizin
    Notizen: We present an analysis of the blind predictions submitted to the fold recognition category for the second meeting on the Critical Assessment of techniques for protein Structure Prediction. Our method achieves fold recognition from predicted secondary structure sequences using hidden Markov models (HMMs) of protein folds. HMMs are trained only with experimentally derived secondary structure sequences of proteins having similar fold, therefore protein structures are described by the models at a remarkably simplified level. We submitted predictions for five target sequences, of which four were later found to be suitable for threading. Our approach correctly predicted the fold for three of them. For a fourth sequence the fold could have been correctly predicted if a better model for its structure was available. We conclude that we have additional evidence that secondary structure information represents an important factor for achieving fold recognition. Proteins, Suppl. 1:123-128, 1997. Published 1998 Wiley-Liss, Inc.This article is a US government work and, as such, is in the public domain in the United States of America.
    Zusätzliches Material: 1 Ill.
    Materialart: Digitale Medien
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