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  • Biochemistry and Biotechnology  (82)
  • Physical Chemistry  (8)
  • Autoradiography  (6)
  • 1
    Digitale Medien
    Digitale Medien
    Estimation of parameters in population models for Schizosaccharomyces pombe from chemostat data (1972)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 14 (1972), S. 915-938 
    Details
    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
    URL: http://dx.doi.org/10.1002/bit.260140605
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  • 2
    Digitale Medien
    Digitale Medien
    Recombinant antineuraminidase single chain antibody: Expression, characterization, and crystallization in complex with antigen (1993)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 16 (1993), S. 57-63 
    Details
    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
    URL: http://dx.doi.org/10.1002/prot.340160107
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  • 3
    Digitale Medien
    Digitale Medien
    Towards meeting the paracelsus challenge: The design, synthesis, and characterization of paracelsin-43, an α-helical protein with over 50% sequence identity to an all-β protein (1996)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 24 (1996), S. 502-513 
    Details
    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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  • 4
    Digitale Medien
    Digitale Medien
    Structural aspects of the functional modules in human protein kinase-Cα deduced from comparative analyses (1996)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 26 (1996), S. 217-235 
    Details
    ISSN: 0887-3585
    Schlagwort(e): catalytic region ; comparative modeling ; cysteine-rich domain ; phosphorylation ; pseudo-substrate specificity ; synaptotagmin ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Medizin
    Notizen: Three-dimensional models of the five functional modules in human protein kinase Cα (PKCα) have been generated on the basis of known related structures. The catalytic region at the C-terminus of the sequence and the N-terminal auto-inhibitory pseudo-substrate have been modeled using the crystal structure complex of cAMP-dependent protein kinese (cAPK) and PKI peptide. While the N-terminal helix of the catalytic region of PKCα is predicted to be in a different location compared with cAPK, the C-terminal extension is modeled like that in the cAPK. The predicted permissive phosphorylation site of PKCα, Thr 497, is found to be entirely consistent with the mutagenesis studies. Basic Lys and Arg residues in the pseudo-substrate make several specific interactions with acidic residues in the catalytic region and may interact with the permissive phosphorylation site. Models of the two zinc-binding modules of PKCα are based on nuclear magnetic resonance and crystal structures of such modules in other PKC isoforms while the calcium phospholipid binding module (C2) is based on the crystal structure of a repeating unit in synaptotagmin I. Phorbol ester binding regions in zinc-binding modules and the calcium binding region in the C2 domain are similar to those in the basis structures. A hypothetical model of the relative positions of all five modules has the putative lipid binding ends of the C2 and the two zinc-binding domains pointing in the same direction and may serve as a basis for further experiments. © 1996 Wiley-Liss, Inc.
    Zusätzliches Material: 10 Ill.
    Materialart: Digitale Medien
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  • 5
    Digitale Medien
    Digitale Medien
    Glucoamylase structural, functional, and evolutionary relationships (1997)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 29 (1997), S. 334-347 
    Details
    ISSN: 0887-3585
    Schlagwort(e): evolution ; glucoamylase ; hydrophobic folding ; protein parsimony analysis ; structure/function ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Medizin
    Notizen: To correlate structural features with glucoamylase properties, a structure-based multisequence alignment was constructed using information from catalytic and starch-binding domain models. The catalytic domain is composed of three hydrophobic folding units, the most labile and least hydrophobic of them being missing in the most stable glucoamylase. The role of O-glycosylation in stabilizing the most hydrophobic folding unit, the only one where thermostabilizing mutations with unchanged activity have been made, is described. Differences in both length and composition of interhelical loops are correlated with stability and selectivity characteristics. Two new glucoamylase subfamilies are defined by using homology criteria. Protein parsimony analysis suggests an ancient bacterial origin for the glucoamylase gene. Increases in length of the belt surrounding the active site, degree of O-glycosylation, and length of the linker probably correspond to evolutionary steps that increase stability and secretion levels of Aspergillus-related glucoamylases. Proteins 29:334-347, 1997. © 1997 Wiley-Liss, Inc.
    Zusätzliches Material: 3 Ill.
    Materialart: Digitale Medien
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  • 6
    Digitale Medien
    Digitale Medien
    Automated docking of monosaccharide substrates and analogues and methyl α-Acarviosinide in the glucoamylase active site (1997)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 27 (1997), S. 235-248 
    Details
    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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  • 7
    Digitale Medien
    Digitale Medien
    Automated docking of glucosyl disaccharides in the glucoamylase active site (1997)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 28 (1997), S. 162-173 
    Details
    ISSN: 0887-3585
    Schlagwort(e): AutoDock ; cellobioside ; disaccharide ; docking ; gentiobioside ; glucoamylase ; kojibioside ; maltoside ; nigeroside ; simulated annealing ; trehalose ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Medizin
    Notizen: To better understand the molecular basis of glucomylase selectivity, low-energy conformers of glucosyl disaccharides obtained from relaxed-residue conformational mapping were flexibly docked into the glucoamylase active site using AutoDock 2.2. This procedure ensures that significant conformational space is searched and can produce bound structures comparable to those obtained by protein crystallography. α-Linked glucosyl disaccharides except α,α-trehalose dock easily into the active site while exclusively β-linked disaccharides do not, explaining why only the former are glucoamylase substrates. The optimized docking modes are similar at the nonreducing end of the different substrates. Individual atomic energies of intermolecular interaction allow the definite identification of key hydroxyl groups for each substrate. This approach confirmed the versatility of the second subsite of the glucoamylase active site in binding different substrates. Proteins 28:162-173, 1997. © 1997 Wiley-Liss Inc.
    Zusätzliches Material: 2 Ill.
    Materialart: Digitale Medien
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  • 8
    Digitale Medien
    Digitale Medien
    1H NMR structure of an antifungal γ-thionin protein SIα1: Similarity to scorpion toxins (1998)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 32 (1998), S. 334-349 
    Details
    ISSN: 0887-3585
    Schlagwort(e): antifungal ; thionin ; NMR ; structure ; scorpion ; toxins ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Medizin
    Notizen: The three-dimensional structure of the Sorghum bicolor seed protein γ-thionin SIα1 has been determined by 2D 1H nuclear magnetic resonance (NMR) spectroscopy. The secondary structure of this 47-residue antifungal protein with four disulphide bridges consists of a three-stranded antiparallel sheet and one helix. The helix is tethered to the sheet by two disulphide bridges which link two successive turns of the helix to alternate residues i, i + 2 in one strand. Possible binding sites for antifungal activity are discussed. The same fold has been observed previously in several scorpion toxins. Proteins 32:334-349, 1998. © 1998 Wiley-Liss, Inc.
    Zusätzliches Material: 10 Ill.
    Materialart: Digitale Medien
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  • 9
    Digitale Medien
    Digitale Medien
    Fold recognition using predicted secondary structure sequences and hidden Markov models of protein folds (1997)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 29 (1997), S. 123-128 
    Details
    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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  • 10
    Digitale Medien
    Digitale Medien
    Localization of 3H-estradiol in the uterus of pregnant and non-pregnant armadillos (1981)
    Springer
    Cell & tissue research 220 (1981), S. 773-780 
    Details
    ISSN: 1432-0878
    Schlagwort(e): Estrogen receptors ; Uterus ; Armadillo ; Autoradiography
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin
    Notizen: Summary The uptake and retention of radiolabeled estradiol by the uterus was examined in the armadillo. One pregnant and two non-pregnant armadillos were treated with 1.4 μg/kg body weight of 3H-estradiol (E2) by injection into the left ventricle, and one non-pregnant animal was injected with both the labeled hormone and 140 μg/kg body weight of unlabeled E2. One and a half hour after injection, the animals were sacrificed and the uteri were removed and processed for autoradiography. In the non-pregnant animals, nuclear localization was observed in the interstitial cells and glandular epithelium of the endometrium and the connective tissue cells and smooth muscle of the myometrium. Additionally, there was a gradation of uptake in the epithelial cells of the endometrium in that the glandular cells of the basal region were heavily labeled, while those cells in the sinusoidal, and luminal regions contained successively less label. The luminal cells were poorly labeled. In the pregnant female, the smooth muscle and glandular cells hypertrophied and their nuclei contained less label than was observed in the non-pregnant animals. The arteries of the myometrium were more easily distinguished in the pregnant animals and the nuclei of the endothelial cells and smooth muscle were more consistently labeled than those of the non-pregnant armadillos.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00210460
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