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  • 1
    Electronic Resource
    Electronic Resource
    Circular dichroism studies of barnase and its mutants: Characterization of the contribution of aromatic side chains (1993)
    s.l. : American Chemical Society
    Biochemistry 32 (1993), S. 10303-10313 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00090a005
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  • 2
    Electronic Resource
    Electronic Resource
    Thermodynamic study of the acid denaturation of barnase and its dependence on ionic strength: Evidence for residual electrostatic interactions in the acid/thermally denatured state (1994)
    s.l. : American Chemical Society
    Biochemistry 33 (1994), S. 8826-8832 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00195a026
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  • 3
    Electronic Resource
    Electronic Resource
    Enzyme-mediated dichloromethane toxicity and mutagenicity of bacterial and mammalian dichloromethane-active glutathione S-transferases (1999)
    Springer
    Archives of toxicology 73 (1999), S. 71-79 
    Details
    ISSN: 1432-0738
    Keywords: Key words Dichloromethane ; Dichloromethane dehalogenase ; Formaldehyde ; Glutathione S-transferase ; Bacterial genotoxicity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The kinetic properties of bacterial and rat liver glutathione S-transferases (GST) active with dichloromethane (DCM) were compared. The theta class glutathione S-transferase (rGSTT1-1) from rat liver had an affinity for dihalomethanes lower by three orders of magnitude (K app 〉 50 mM) than the bacterial DCM dehalogenase/GST from Methylophilus sp. DM11. Unlike the bacterial DCM dehalogenase, the rat enzyme was unable to support growth of the dehalogenase minus Methylobacterium sp. DM4-2cr mutant with DCM. Moreover, the presence of DCM inhibited growth with methanol of the DM4-2cr transconjugant expressing the rat liver GSTT1-1. In Salmonella typhimurium TA1535, expression of rat and bacterial DCM-active GST from a plasmid in the presence of DCM yielded up to 5.3 times more reversions to histidine prototrophy in the transconjugant expressing the rat enzyme. Under the same conditions, however, GST-mediated conversion of DCM to formaldehyde was lower in cell-free extracts of the transconjugant expressing the rat GSTT1 than in the corresponding strain expressing the bacterial DCM dehalogenase. This provided new evidence that formaldehyde was not the main toxicant associated with GST-mediated DCM conversion, and indicated that an intermediate in the transformation of DCM by GST, presumably S-chloromethylglutathione, was responsible for the observed effects. The marked differences in substrate affinity of rat and bacterial DCM-active GST, as well as in the toxicity and genotoxicity associated with expression of these enzymes in bacteria, suggest that bacterial DCM dehalogenases/GST have evolved to minimise the toxic effects associated with glutathione-mediated catalysis of DCM conversion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002040050589
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  • 4
    Electronic Resource
    Electronic Resource
    Microbes, enzymes and genes involved in dichloromethane utilization (1994)
    Springer
    Biodegradation 5 (1994), S. 237-248 
    Details
    ISSN: 1572-9729
    Keywords: Dichloromethane ; dichloromethane dehalogenase ; glutathione S-transferase ; methylotrophic bacteria ; Methylobacterium sp. ; Methylophilus sp.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Energy, Environment Protection, Nuclear Power Engineering , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Dichloromethane (DCM) is efficiently utilized as a carbon and energy source by aerobic, Gram-negative, facultative methylotrophic bacteria. It also serves as a sole carbon and energy source for a nitrate-respiringHyphomicrobium sp. and for a strictly anaerobic co-culture of a DCM-fermenting bacterium and an acetogen. The first step of DCM utilization by methylotrophs is catalyzed by DCM dehalogenase which, in a glutathione-dependent substitution reaction, forms inorganic chloride and S-chloromethyl glutathione. This unstable intermediate decomposes to glutathione, inorganic chloride and formaldehyde, a central metabolite of methylotrophic growth. Genetic studies on DCM utilization are beginning to shed some light on questions pertaining to the evolution of DCM dehalogenases and on the regulation of DCM dehalogenase expression. DCM dehalogenase belongs to the glutathione S-transferase supergene family. Analysis of the amino acid sequences of two bacterial DCM dehalogenases reveals 56% identity, and comparison of these sequences to those of glutathione S-transferases indicates a closer relationship to class Theta eukaryotic glutathione S-transferases than to a number of bacterial glutathione S-transferases whose sequences have recently become available.dcmA, the structural gene of the highly substrate-inducible DCM dehalogenase, is carried in most DCM utilizing methylotrophs on large plasmids. InMethylobacterium sp. DM4 its expression is governed bydcmR, a regulatory gene located upstream ofdcmA. dcmR encodes atrans-acting factor which negatively controls DCM dehalogenase formation at the transcriptional level. Our working model thus assumes that thedcmR product is a repressor which, in the absence of DCM, binds to the promoter region ofdcmA and thereby inhibits initiation of transcription.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00696462
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  • 5
    Electronic Resource
    Electronic Resource
    The Construction of New Proteins. Part IIIPart 11: [4]. Artificial folding units by assembly of amphiphilic secondary structures on a template (1988)
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 71 (1988), S. 835-847 
    Details
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A new general strategy for the construction of artificial proteins with predetermined tertiary structure is presented. Amphiphilic α-helix and β-sheet-forming oligopeptides are assembled on a multifunctional ttemplate molecule which directs the peptide blocks to adopt characteristic folding topologies. The design, synthesis, and conformational properties of these template-assembled synthetic proteins (TASP) are exemplified for βαβ-, α-helix-bundle- and β-barrel-like tertiary structures using specially designed oligopeptides as template molecules. In contrast to linear polypeptide chains of comparable molecular weights, these conceptually novel marcromolecules are readily accessible to chemical synthesis and exhibit excellent solubility in a number of solvents. Experimental evidence is provided for a template-induced intramolecular folding to secondary and tertiary structures in aqueous solutions. This approach opens new prospects for the chemical construction of biomacromolecules with tailormade structural and functional properties.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/hlca.19880710419
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  • 6
    Electronic Resource
    Electronic Resource
    Ein chemischer Weg zu neuen Proteinen - Templat-assoziierte synthetische Proteine (TASP)In memoriam Emil Thomas Kaiser. (1989)
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 101 (1989), S. 551-571 
    Details
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Fortschritte in den Methoden der Chemie und der Molekularbiologie veranlassen uns, einige Strukturprinzipien von Proteinen im Hinblick auf die Möglichkeit, künstliche Proteine zu entwerfen, erneut zu betrachten. Die chemische Synthese von Polypeptiden und die ortsspezifische Mutagenese von Proteinen haben sich zu Standardmethoden entwickelt und den Weg zur Konstruktion neuer Proteine geebnet. Obwohl in den vergangenen Jahren wesentliche Einblicke in den räumlichen Bau von natürlichen Proteinen gewonnen werden konnten, sind wir heute noch weit davon entfernt, nicht-natürliche Proteine mit maßgeschneiderten strukturellen und funktionellen Eigenschaften zu konstruieren - zweifellos ein Ziel von weitreichender wissenschaftlicher und ökonomischer Tragweite. Die entscheidende Hürde liegt weniger in der Synthese dieser Moleküle per se als vielmehr in einem besseren Verständnis des komplizierten Faltungsprozesses von Polypeptidketten in eine definierte räumliche Struktur. Kann der Chemiker seine Synthesewerkzeuge dazu einsetzen, diese als „Faltungsproblem“ bekanntgewordene Klippe des Neuentwurfs von Proteinen („de-novo-Design“) zu umschiffen? Im vorliegenden Bericht wird das kürzlich in unserem Laboratorium entwickelte TASP-Konzept vorgestellt, das einen synthetischen Zugang zu künstlichen Proteinen mit vorausbestimmter dreidimensionaler Struktur eröffnet. Damit ist ein erster Schritt auf dem Weg zu neuen Proteinen mit interessanten funktionellen Eigenschaften getan.
    Additional Material: 24 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ange.19891010504
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  • 7
    Electronic Resource
    Electronic Resource
    Synthetic peptide and template-assembled synthetic protein models of the hen egg white lysozyme 87-97 helix: Importance of a protein-like framework for conformational stability in a short peptide sequence (1993)
    New York : Wiley-Blackwell
    Biopolymers 33 (1993), S. 389-400 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: In the native structure of hen egg white lysozyme (HEL), the amino acid sequence 87-97 (HEL 87-97) forms an amphiphilic helix, with hydrophilic residues in the sequence directed toward the solvent. A synthetic version of the HEL 87-97 sequence (with the cysteine corresponding to position 94 of HEL replaced by alanine) displays conformational features in solution typical of an unordered structure as judged by CD. However, various modifications in the sequence result in increased helix-forming potential of the HEL 87-97 analogues. Further stabilization of the helical conformation in the most helical analogue of the HEL 87-97 sequence is obtained when 4 copies of this peptide sequence are coupled on a peptide carrier molecule following the template-assembled synthetic protein (TASP) approach M. Mutter and S. Vuilleumier (1989) Angew. Chem. Int. Ed. Engl., Vol. 28, pp. 535-554 “A Chemical Approach to Protein Design-Template-Assembled Synthetic Proteins (TASP).” This suggests that long-range interactions of the peptide with its environment contribute to conformational stability in short peptide sequences. TASP molecules may prove useful for the study of the factors that determine secondary structure formation in short peptides by providing a protein-like framework. © 1993 John Wiley & Sons, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360330307
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  • 8
    Electronic Resource
    Electronic Resource
    Approaches to Synthetic Vaccines Design of Epitope-Containing Amphiphilic Peptides Matching the Antigenic Structure in the Native Protein (1986)
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 69 (1986), S. 985-995 
    Details
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A general procedure for the design of synthetic vaccines with the retained conformational features of protein antigenic determinants is described. This new concept emerges from detailed studies on the relationship between primary sequence and secondary structure formation of synthetic peptides and takes advantage of the amphiphilic nature of epitope-containing peptide segments in the native protein to accomplish structural modifications. These segments, for example amphiphilic helices or β-sheets, are stabilized by the insertion of secondary structure-inducing amino-acid residues on the hydrophobic part of the peptide without affecting the spatial arrangement of functional residues on the hydrophilic side. The availability of amphiphilic peptides with tailor-made conformational properties, e.g. helices, β-sheets, and, moreover, assemblies of these blocks to structures of higher order (‘folding units’), allows the presentation and stabilization of continuous as well as discontinuous epitopes by this approach. This strategy is exemplified for the case of two discontinuous epitopes taken from lysozyme, which are matched to host molecules with adequate conformational features by the help of computer-assisted molecular modelling. The implications of this new concept for the design of synthetic vaccines are discussed with special emphasis to the important role of peptide synthesis and chemical structure modification.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/hlca.19860690505
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  • 9
    Electronic Resource
    Electronic Resource
    A Chemical Approach to Protein Design - Template-Assembled Synthetic Proteins (TASP)In memoriam Emil Thomas Kaiser (1989)
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 28 (1989), S. 535-554 
    Details
    ISSN: 0570-0833
    Keywords: Protein design ; Proteins ; Template synthesis ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Advances in methodology in both chemistry and molecular biology allow us to take a fresh look at protein science. Chemical synthesis of peptides and site-directed mutagenesis are now standard research tools, paving the way for the construction of new proteins with tailor-made structural and functional properties. The decisive hurdle on the way lies not in the synthesis of the molecules proper but rather in a better understanding of the complex folding pathways of polypeptide chains into spatially well-defined structures. Can the chemist use his synthetic tools to bypass the notorious “folding problem?” In this article, we present a new approach developed in our laboratory, which opens a chemical route to artificial proteins with predetermined three-dimensional structures, allowing a first step towards the synthesis of new proteins with functional properties.
    Additional Material: 24 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/anie.198905353
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