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  • 1
    Electronic Resource
    Electronic Resource
    Photoexcitations in linear trans-quinacridone (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Advanced Materials for Optics and Electronics 7 (1997), S. 35-38 
    Details
    ISSN: 1057-9257
    Keywords: photoluminescence ; time-resolved fast spectrocopy ; photoinduced absorption spectroscopy ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Electrical Engineering, Measurement and Control Technology , Physics
    Notes: We have studied the photophysics of linear trans-quinacridone films by applying a variety of transient and continuous wave photomodulation techniques. Our experimental results demonstrate the ultrafast formation of excimer species which are responsible for the emission. The excimer decay kinetics seems to suggest a predominantly charge transfer character of these emitting species. This is consistent with the long-lived states which we detected on the millisecond time scale. © 1997 John Wiley & Sons, Ltd.
    Additional Material: 4 Ill.
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  • 2
    Electronic Resource
    Electronic Resource
    Photoexcitations in linear trans-quinacridone (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Advanced Materials for Optics and Electronics 7 (1997), S. 83-86 
    Details
    ISSN: 1057-9257
    Keywords: photoluminescence ; time-resolved fast spectrocopy ; photoinduced absorption spectroscopy ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Electrical Engineering, Measurement and Control Technology , Physics
    Notes: We have studied the photophysics of linear trans-quinacridone films by applying a variety of transient and continuous wave photomodulation techniques. Our experimental results demonstrate the ultrafast formation of excimer species which are responsible for the emission. The excimer decay kinetics seems to suggest a predominantly charge transfer character of these emitting species. This is consistent with the long-lived states which we detected on the millisecond time scale. © 1997 John Wiley & Sons, Ltd.
    Additional Material: 4 Ill.
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  • 3
    Electronic Resource
    Electronic Resource
    Electron transport in acceptor doped polymers: The role of group dipole moments (1995)
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part B: Polymer Physics 33 (1995), S. 2143-2149 
    Details
    ISSN: 0887-6266
    Keywords: diphenoquinones ; disorder-controlled hopping ; doped polymers ; electron transport ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: Electron mobilities have been measured in poly(styrene) doped with an isomer mixture of two diphenoquinone (DPQ) compounds over a range of fields, temperatures, and DPQ concentrations. The results are interpreted within the framework of a formalism based on disorder, due to Bässler and coworkers. The formalism is based on the assumption that charge transport occurs by hopping through a manifold of localized states with superimposed energetic and positional disorder. The key parameter of the formalism is the energy width of the hopping site manifold. For DPQ doped poly(styrene), the energy width is 0.118 eV and independent of the intersite distance or DPQ concentration. The width can be described by a model based on dipolar disorder, if it is assumed that the fluctuations of hopping site energies are due to group dipole moments associated with the carbonyl groups of the DPQ molecules. The interpretation of the experimental results leads to the further conclusion that polaronic effects need not be invoked to explain transport phenomena in this class of doped polymers. © 1995 John Wiley & Sons, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/polb.1995.090331505
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  • 4
    Electronic Resource
    Electronic Resource
    Selective production of carbon structures by non-equilibrium techniques (1997)
    Weinheim : Wiley-Blackwell
    Chemical Vapor Deposition 3 (1997), S. 301-306 
    Details
    ISSN: 0948-1907
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cvde.19970030603
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  • 5
    Electronic Resource
    Electronic Resource
    Bioactive peptides: Conformational studies of [TYR4] cyclolinopeptide A (1995)
    New York : Wiley-Blackwell
    Biopolymers 36 (1995), S. 453-460 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The solid state conformational analysis of [Tyr4] cyclolinopeptide A has been carried out by x-ray diffraction studies. The crystal structure of the monoclinic form, grown from a dioxane-water mixture [a = 9.849 (5) Å, b = 20.752 (4) Å, c = 16.728 (5) Å, β = 98.83 (3)°, space group P21, Z = 2], shows the presence of five intramolecular N-H- O=C hydrogen bonds, with formation of one C17 ring structure, one α-turn (C13), one inverse γ-turn (C7), and two β-turns (C10, one of type III and one of type 1). The Pro1-Pro2 peptide unit is cis (ω = 5°) all others are trans. The structure is almost superimposable with that of cyclolinopeptide A. The rms deviation for the atoms of the backbones is on the average 0.33 Å. © 1995 John Wiley & Sons, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360360408
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  • 6
    Electronic Resource
    Electronic Resource
    Peptides containing the sulfonamide junction: Synthesis, structure, and conformation of Z-Tau-Pro-Phe-NHiPr (1997)
    New York : Wiley-Blackwell
    Biopolymers 41 (1997), S. 555-567 
    Details
    ISSN: 0006-3525
    Keywords: sulfonamido-peptides ; taurine ; β- and γ-turns ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The taurine (Tau) containing tripeptide derivative Z-Tau-Pro-Phe-NHiPr (1) has been synthesized as suitable sulfonamido-pseudopeptide model to investigate formation and conformational properties of folded secondary structures stabilized by intramolecular H bonds directly involving the sulfonamide junction. In the crystal the pseudopeptide 1 adopts a type I β-turn with the Pro and Phe residues located at the (i + 1) and (i + 2) corner positions, respectively. The turn is stabilized by a 4 → 1 H bond engaging one of the SO2 oxygen atoms and the isopropylamide NH. In CDCl3 solution the β-turn folding is accompanied by a γ-turn centered at the Pro and involving a 3 → 1 H bond between the SO2 and the Phe NH. A comparison of the structural and conformational properties found in 1 with those of the already known sulfonamido-pseudopeptides, with particular reference to the models containing the Tau-Pro junction, is also reported. © 1997 John Wiley & Sons, Inc. Biopoly 41: 555-567, 1997.
    Additional Material: 7 Ill.
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  • 7
    Electronic Resource
    Electronic Resource
    Specific interaction between cyclophilin and cyclic peptides (1995)
    New York : Wiley-Blackwell
    Biopolymers 36 (1995), S. 273-281 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Cyclophilin A, a peptidyl-prolyl cis-trans isomerase that catalyzes the otherwise slow isomerization of Xaa-Pro imidic bond, specifically binds the immunosuppressant cyclosporin A. Herein we reportevidence on binding of cyclolinopeptide A and its synthetic analogue, [Aib5,6-D-Ala8] cyclolinopeptide, to bovine cyclophilin A. Binding experiments were monitored by fluorescence. CD, and second-derivative spectroscopies, evidencing no remarkable rearrangement of protein structure organization. The possibility that cyclolinopeptide A could act as a substitute of cyclosporin A in the immunosuppression modulation is also briefly discussed. © 1995 John Wiley & Sons, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360360303
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  • 8
    Electronic Resource
    Electronic Resource
    Conformational studies of heterochiral peptides with diastereoisomeric residues: Crystal and molecular structures of linear dipeptides derived from leucine, isoleucine, and allo-isoleucine (1995)
    New York : Wiley-Blackwell
    Biopolymers 36 (1995), S. 401-408 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The x-ray diffraction analyses of three N- and C-terminally blocked L, D dipeptides, namely t-Boc-D-Leu-L-Leu-OMe (1), t-Boc-L-Ile-D-alle-OMe (2), and t-Boc-D-aIle-L-Ile-OMe (3) containing enantiomeric or diastereomeric amino acid residues have been carried out. The structures were determined by direct methods and refined anisotropically to final R factors of 0.077. 0.058. and 0.072 for (1) (2) and (3), respectively.Peptides 1-3 all assume a similar U-shaped structure with φ and ψ torsion angles cosrresponding to one of the possible calculated minimum energy regions (regions E and G for L residues, and F*. D* and H* for D residues). The peptide backbones of 1-3 are almost super-imposable [provided that the appropriate inversion of the chiral centers of (2) is made].Side-chain conformations of Leu residues in peptide (1) are g- (tg-) for the L-Leu residue and the mirrored g+ (tg+) for the D-Leu residue; however, in peptides (2) and (3) the conformations of the isoconfiguralional side chains of the Ile or allo-Ile residues are (g-t) t and (tg+) tfor the L-Ile and the D-allo-Ile moieties, respectively. In all cases, these conformations correspond to the more populated conformers of β-branched residues statistically found in crystal structures of small peptides.The results seem to indicate that, at least in short peptides with enantiomeric or diastereoisomeric residues, the change in chirality in the main-chain atoms perturbs the backbone conformation to a lesser extent and the side chain conformation to a greater extent. © 1995 John Wiley & Sons, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360360403
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  • 9
    Electronic Resource
    Electronic Resource
    Solution and solid state structure of an aib-containing cyclodecapeptide inhibiting the cholate uptake in hepatocytes (1996)
    New York : Wiley-Blackwell
    Biopolymers 40 (1996), S. 465-478 
    Details
    ISSN: 0006-3525
    Keywords: cyclic decapeptides ; cyclolinopeptide A ; x-ray ; nmr ; conformation ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The conformational analysis of synthetic cyclodecapeptide c(Pro-Phe-Phe-Aib-Leu)2 related to the cyclolinopeptide A, in the solid state and solution, has been carried out by x-ray diffraction and nmr spectroscopy. The structure of the monoclinic form obtained from methanol [a = 11.351(5) Å, b = 27.455(2) Å, c = 12.716(8) Å, β = 99.65(3)°; space group P21; Z = 2] shows the presence of six intramolecular NH···CO hydrogen bonds, with formation of four turns (three of type I and one of type III) and two C16 ring structures. All peptide units are trans. The solution structure, as found by nmr, indicates that, at room temperature, the peptide is conformationally homogeneous; the structure determined is perfectly symmetrical and topologically similar to that found in the solid state. The cyclodecapeptide exhibits similar biological activity to cyclolinopeptide A. © 1997 John Wiley & Sons, Inc. Biopoly 40: 465-478, 1996
    Additional Material: 7 Ill.
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  • 10
    Electronic Resource
    Electronic Resource
    Solution conformational preferences of a peptidic analogue of a natural macrolide (1997)
    New York : Wiley-Blackwell
    Biopolymers 42 (1997), S. 349-361 
    Details
    ISSN: 0006-3525
    Keywords: cyclic peptides ; molecular dynamics ; nmr ; conformation ; FK506 ; FK506 binding proteins ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The conformational behavior in solution of a cyclic peptide with sequence cyclo-(Pro1-Pro2-Dab3 (cHexA)ψ[N7HCO]-Leu4ψ[NHCO]-Suc5-Gly6-) has been throughly investigated with the combined use of nmr and molecular dynamic techniques. The compound, which has been modeled to mimic the FK506 macrolide bound to the FK506 binding protein structure, can be considered as a peptidic analogue of the FK506 system.The synthesis was carried out on a phenylacetoamidomethyl resin using an appropriate protocol for the peptide chain elongation. The conformational properties of the cyclic hexapeptide were studied in DMSO and water. The nmr data in DMSO and restrained molecular dynamics simulations show the presence of two contiguous cis peptide bonds involving the -Gly-Pro-Pro- segment. This segment in water exhibits conformational heterogeneity presenting at least two distinct conformational families, characterized the first by cis-cis and the second by a trans-cis Gly-Pro-Pro configuration; the trans-cis isomer was fully characterized. © 1997 John Wiley & Sons, Inc. Biopoly 42: 349-361, 1997
    Additional Material: 6 Ill.
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