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  • 11
    Electronic Resource
    Electronic Resource
    Linear oligopeptides. 99. An infrared absorption method to titrate quantitatively the extent of self-association in peptides (1984)
    s.l. : American Chemical Society
    Journal of the American Chemical Society 106 (1984), S. 1455-1457 
    Details
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ja00317a044
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  • 12
    Electronic Resource
    Electronic Resource
    Nitrogen-15 magnetic resonance spectroscopy. Natural-abundance spectra of isomeric homooligopeptides of L-norvaline and L-valine to the tetramers (1980)
    s.l. : American Chemical Society
    The @journal of organic chemistry 45 (1980), S. 288-290 
    Details
    ISSN: 1520-6904
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jo01290a017
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  • 13
    Electronic Resource
    Electronic Resource
    Peptide helices as rigid molecular rulers: A conformational study of isotactic homopeptides from α-methyl-α-isopropylglycine, [L-(αMe)Val]nLinear Oligopeptides, Part 360. Part 359: A. Bianco, M. Maggini, G. Scorrano, C. Toniolo, G. Marconi, C. Villani, M. Prato, J. Am. Chem. Soc. 1996, 118, 4072-4080. (1996)
    Weinheim : Wiley-Blackwell
    Chemistry - A European Journal 2 (1996), S. 1104-1111 
    Details
    ISSN: 0947-6539
    Keywords: amino acids ; conformation ; helices ; molecular rulers ; oligopeptides ; structure elucidation ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Terminally blocked, isotactic homopeptides from the sterically demanding α-methylvaline of general formula Y-[L-(αMe)Val]n-OtBu (Y = Z, pBrBz, Ac; n = 2-8) have been prepared step-by-step in solution and fully characterized. The conformations preferred in solution (β-turn and right-handed 310-helix) have been assessed by FT-IR, 1H NMR and CD spectroscopy. The molecular and crystal structures of the Z-protected trimer, hexamer, heptamer and octamer have been determined by X-ray diffraction. In the crystal state, while the trimer is folded in a type III β-turn conformation, the longest homopeptides form well-developed, regular, right-handed 310-helices. The screw sense in the helix of the pBrBz-blocked octamer has been confirmed to be right-handed by solid-state and solution CD spectroscopy. The possible exploitation of these peptide helices as rigid and precise molecular rulers is discussed.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/chem.1460020909
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  • 14
    Electronic Resource
    Electronic Resource
    Linear oligopeptides, 70Part 69: Cf.1.. Study of the relationship between conformation and nature of the side chain: Homologous series derived from α-amino acid residues with linear hydrocarbon side chains (1981)
    New York : Wiley-Blackwell
    Die Makromolekulare Chemie 182 (1981), S. 3149-3162 
    Details
    ISSN: 0025-116X
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: A series of N- and C-protected L-α-aminobutyric acid homo-oligopeptides from dipeptide through heptapeptide was synthesized by the dicyclohexylcarbodiimide and acyl azide coupling methods. The monodisperse peptides were characterized and found to be chemically and optically pure. By means of infrared absorption and circular dichroism in the vacuum ultraviolet (150 nm) the occurrence of the intermolecular β-conformation in the higher oligopeptides in the solid state was ascertained. In solvents of low polarity at high dilution the amount of intramolecularly hydrogen-bonded folded structure formation was established as a function of peptide chain length. Unordered and intermolecular β-structures were found in alcohols and in water/2,2,2-trifluoroethanol mixtures. The results obtained are compared with those already published of other homologous peptide series derived from L-α-amino acid residues with linear hydrocarbon side chains, namely alanine, norvaline, and norleucine. Analogies and differences with the series from β- and γ-branched residues are also discussed.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/macp.1981.021821121
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  • 15
    Electronic Resource
    Electronic Resource
    Conformational properties of homo-oligo(L-leucine)s in solution. Comparison with isoleucines (1974)
    New York : Wiley-Blackwell
    Die Makromolekulare Chemie 175 (1974), S. 1665-1668 
    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.1974.021750525
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  • 16
    Electronic Resource
    Electronic Resource
    Structural aspects of small peptides. Synthesis and characterization of protected homo-oligomers derived from L-alanine (1975)
    New York : Wiley-Blackwell
    Die Makromolekulare Chemie 176 (1975), S. 2535-2545 
    Details
    ISSN: 0025-116X
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Description / Table of Contents: Eine Reihe von geschützten L-Alanin-Homo-Oligomeren vom Dimeren bis zum Heptameren wurde durch die Dicyclohexylcarbodiimid- und Azidkupplung dargestellt. Als N-Schutzgruppe wurde der tert-Butoxycarbonylrest und als C-Schutzgruppe die Methylestergruppe verwendet. Die so synthetisierten molekulareinheitlichen Oligomeren wurden charakterisiert und erwiesen sich als chemisch rein. Die polarimetrische Untersuchung in einem denaturierenden Lösungsmittel zeigte, daß alle Reaktionen unter vollständiger Erhaltung der Konfiguration erfolgten. Außerdem wurde die Abhängigkeit der experimentell gefundenen Werte der Molekularrotation der innenständigen L-Alaninreste bei 589 nm im statistischen Knäuel von der Struktur der Endgruppen und dem Lösungsmittel besonders herausgestellt.
    Notes: A series of protected L-alanine homo-oligomers from dimer to heptamer was prepared by the dicyclohexylcarbodiimide and acyl azide coupling methods. In the course of the synthetic approach tert-butoxycarbonyl as the N-protecting and methyl ester as the C-protecting end groups were employed. The monodisperse oligomers prepared in this manner were characterized and found to be chemically pure. A polarimetric investigation in a structure disrupting solvent also indicated that all reactions proceeded with complete retention of the configuration. In addition, the dependence of the experimental molar rotation values at 589 nm of L-alanine internal residues in a polypeptide in a statistical coil conformation on the end groups of the molecule and the solvent is emphasized.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/macp.1975.021760906
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  • 17
    Electronic Resource
    Electronic Resource
    Structural aspects of small peptides. A circular dichroism study of monodisperse protected homo-oligomers derived from L-alanine (1975)
    New York : Wiley-Blackwell
    Die Makromolekulare Chemie 176 (1975), S. 2547-2558 
    Details
    ISSN: 0025-116X
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Description / Table of Contents: Die Konformation einer Reihe von molekulareinheitlichen, chemisch und optisch reinen geschützten L-Alanin-Homo-Oligomeren mit der allgemeinen Formel BOC—(L-Ala)n—OCH3 (n=2-7) wurden in Lösung mit Hilfe der CD-Methode untersucht. Es wurde gefunden, daß diese Peptide in einem hauptsächlich β-assoziierten statistischen Knäuel oder in partiell α-helicalen Konformationen auftreten können, abhängig vom Molekulargewicht, Lösungsmittel, Temperatur und Oligomerenkonzentration. Die β-Struktur, die im Bereich 5≤n≤7 in 2,2,2-Trifluoräthanol (TFE), TFE-Wasser 20:80 (V/V), Methanol und Äthanol auftrat, konnte durch Verdünnung oder Temperaturerhöhung zerstört werden. In verdünnter TFE-Lösung wurde die Tendenz des Heptameren zur Kettenfaltung gefunden. In 1,1,1,3,3,3-Hexafluorpropan-2-ol und Hexafluoraceton-ses-quihydrat treten alle Oligomeren jedoch ausschließlich in einer ungeordneten Konformation auf.
    Notes: The conformational properties in solution of a series of monodisperse, chemically and optically pure protected L-alanine homo-oligomers, having the general formula BOC—(L-Ala)n—OCH3 (n = 2-7), were investigated using essentially the CD technique. This study demonstrates that these peptides may exist in predominantly β-associated, statistical coil, or partially α-helical conformations depending upon molecular weight, solvent, temperature, and oligomer concentration. The β-structure, which appears in the range 5≤n≤7 in 2,2,2-trifluoroethanol (TFE), TFE-water 20:80 (v/v), methanol, and ethanol could be destroyed by dilution or by increasing the temperature. In diluted TFE solutions, the tendency of the heptamer to form folded species could be detected. In 1,1,1,3,3,3-hexafluoropropan-2-ol and hexafluoroacetone sesquihydrate, however, all oligomers exist essentially in an unordered conformation.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/macp.1975.021760907
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  • 18
    Electronic Resource
    Electronic Resource
    Linear oligopeptides, 29.Part 28: cf.1. Infrared conformational analysis of homo-oligopeptides in the solid state and in solution (1976)
    New York : Wiley-Blackwell
    Die Makromolekulare Chemie 177 (1976), S. 1477-1492 
    Details
    ISSN: 0025-116X
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Description / Table of Contents: Die IR-Spektren von 8 Reihen von molekulareinheitlichen, chemisch und optisch reinen, geschützten linearen Homo-Oligopeptiden mit der allgemeinen Formel Boc(—L—X)n—OMe (mit X = Ala, Nva, Val, Leu, Ile, Phe, Met, Cys(Me) und n = 2-7) wurden durch IR-Absorptionsspektroskopie im festen Zustand und in Lösung untersucht. Die Messungen im festen Zustand ergaben, daß alle Pentameren und höheren Oligomeren hauptsächlich eine β-Form einnehmen. Trimere und Tetramere bestehen danach aus Mischungen von β- und ungeordneten Strukturen, während in den Dimeren die ungeordnete Struktur vorherrscht. Das Auftreten der ungewöhnlichen intermolekularen parallelen βKonformation wird für HCl·H(—L—X)7—OMe (mit X = Val, Ile, Phe) vorgeschlagen. Außerdem wurde die Absorption im Gebiet der N—H-Valenzschwingung in Abhängigkeit von der Konzentration in Deuterochloroform bestimmt. Diese Konformationsanalyse in Lösung zeigte, daß ein hoher Gehah an Strukturen mit intramolekularen Wasserstoffbrücken in allen Homo-Tetrameren vorliegt, mit Ausnahme der Derivate mit β-verzweigten Aminosäureresten (Valin, Isoleucin). Der Effekt eines Schwefelatoms und eines aromatischen Rings in der Seitenkette (S-Methplcystein - Methionin - und Phenylalanin-Peptide) auf die Stabilitlt der gefalteten Formen wird ebenfalls diskutiert.
    Notes: The IR spectra of eight series of monodisperse, chemically and optically pure, protected linear homo-oligopeptides having the general formula Boc(—L—X)n—OMe, where X = Ala, Nva, Val, Leu, Ile, Phe, Met, Cys(Me), and n = 2-7, were investigated by IR absorption spectroscopy in the solid state and in solution. The measurement in the solid state indicate that all pentamers and higher oligomers assume essentially a β-form; trimers and tetramers present evidence of mixtures of β- and unordered structures, while in dimers the unordered structure is largely predominant. The occurrence of the unusual intermolecular β-parallel conformation was suggested for HCl·H(—L—X)7—OMe, where X = Val, Ile, and Phe. Further, the absorbance in the N—H stretching region was determined as a function of concentration in deuterochloroform. This conformational analysis in solution showed that a high content of intramolecularly hydrogen-bonded forms exist in all homo-tetramers with the exception of those derived from the β-branched amino acid residues, valine and isoleucine. The effect of the presence of a sulfur atom or an aromatic ring in the amino acid side chain (S-methyl cysteine, methionine, and phenylalanine peptides) on the stability of the folded forms is also discussed.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/macp.1976.021770519
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  • 19
    Electronic Resource
    Electronic Resource
    Solid state investigation on the homo-oligopeptide Boc—(L-Ala)6—OCH3 by X-rays (1978)
    New York : Wiley-Blackwell
    Die Makromolekulare Chemie 179 (1978), S. 2803-2806 
    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.1978.021791126
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  • 20
    Electronic Resource
    Electronic Resource
    Linear oligopeptides, 55.Part 54: cf.1. Infrared conformational analysis of polyethyleneglycol-bound alanine and valine homo-L-oligopeptides in the solid state and in solution (1979)
    New York : Wiley-Blackwell
    Die Makromolekulare Chemie 180 (1979), S. 1293-1304 
    Details
    ISSN: 0025-116X
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: The IR absorption properties of three series of monodisperse, chemically and optically pure, PEG-bound linear homo-oligopeptides having the general formula t-Boc-(L-Ala-)1-8Gly-OPEG, t-Boc-(L-Val-)1-7Gly-OPEG and t-Boc-(L-Val-)2-8Gly-OPEG-M were investigated in the solid state and in solution. In the latter case the study was extended to solvents of largely different polarity and different concentrations. In the solid state the Ala and Val peptides from n = 5 to n = 8 assume essentially a β-structure. The occurrence of the unusual parallel-chain β-conformation was suggested for the N-deblocked Val highest peptides. The conformational analysis in deuterochloroform at high dilution showed that a much higher content of intramolecularly H-bonded forms exist in Ala4 than in the Val4 peptides. At higher concentrations chain length, solvent, and side chain effects are all operative in determining the extent of peptide association. The influence of the bi- and monofunctional polymeric supports on the conformational properties of the Ala and Val homo-oligopeptide series is also discussed. Finally, preliminary results on the relationship between reactivity of the polymer-bound growing peptide chain during the step-by-step synthesis and peptide conformation are reported.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/macp.1979.021800515
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