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  • 1
    Electronic Resource
    Electronic Resource
    Effect of phenyl ring position in the Cα-methylated α-amino acid side chain on peptide preferred conformation (1996)
    New York : Wiley-Blackwell
    Biopolymers 40 (1996), S. 523-527 
    Details
    ISSN: 0006-3525
    Keywords: conformational analysis, of peptides ; disubstituted glycines, peptides rich in ; Fourier transform in absorption, of peptides ; 310-helical conformation, in peptides ; Cα-methylated α-amino acids, peptides rich in ; nmr, of peptides ; peptide conformation ; x-ray diffraction, of peptides ; β-turn conformation, of peptides ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The preferred conformations of Cα-methyl phenylglycine, Cα-methyl phenylalanine, and Cα-methyl homophenylalanine residues, as determined in model peptides (including homopeptides) by Fourier transform ir absorption, 1H-nmr, CD, and x-ray diffraction techniques, are compared with the aim of investigating the effect of phenyl ring position in the Cα-methylated amino acid side chain. This study shows that (a) β-turn and 310-helical structures are preferentially adopted by peptides rich in these Cα-methylated, aromatic α-amino acids and (b) turn and helix handedness is critically biased by the position of side-chain branching. © 1997 John Wiley & Sons, Inc. Biopoly 40: 523-527, 1996
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
  • 2
    Electronic Resource
    Electronic Resource
    Infrared and Raman study in the solid state of fully protected, monodispersed homooligopeptides of L-valine, L-isoleucine, and L-phenylalanine (1979)
    New York : Wiley-Blackwell
    Biopolymers 18 (1979), S. 411-424 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: An ir-absorption and Raman-scattering study, in the solid state, has been carried out on monodispersed, N- and C-protected homooligopeptides (number of residues, n, from 2 to 7) of L-valine, L-isoleucine, and L-phenylalanine. The amide I, II, III, V, and vNH regions have been examined. Some deuterated (ND) samples have been examined to complete the assignments. L-Phenylalanine dipeptide displays spectral characteristics compatible with the parallel β-structure; L-isoleucine and L-valine dipeptides are probably in a distorted structure. A mixture of parallel and antiparallel extended chains cannot be excluded for the peptides with n = 3. In the amide I region the spectra of peptides with n ≥ 4 show the existence of the β-conformation. The problem of chain orientation within the pleated-sheet structure is discussed on the basis of a recent theoretical treatment of vibrational interactions of the amide I mode.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1979.360180216
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Preferred conformation of peptides rich in alicyclic Cα,α-disubstituted glycines (1996)
    New York : Wiley-Blackwell
    Biopolymers 40 (1996), S. 519-522 
    Details
    ISSN: 0006-3525
    Keywords: conformational analysis, of peptides ; disubstituted glycines, peptides rich in ; Fourier transform ir absorption, of peptides ; 310-helical conformation, in peptides ; Cα-methylated α-amino acids, peptides rich in ; nmr, of peptides ; peptide conformation ; x-ray diffraction, of peptides ; β-turn conformation, in peptides ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The conformational preferences of the alicyclic Cα,α-disubstituted glycines Acnc (1-amino-1-cycloalkane-carboxylic acid; n = 4, 7, 9, 12) were assessed in selected model compounds, including homopeptides and Ala (or Aib, α-aminoisobutyric acid)/Acnc peptides containing a small total number of residues, by Fourier transform ir absorption, 1H-nmr, and x-ray diffraction analyses. The results obtained indicate that β-turn and 310-helical structures are preferentially adopted by short peptides rich in these cycloaliphatic α-amino acids. © 1997 John Wiley & Sons, Inc. Biopoly 40: 519-522, 1996
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
  • 4
    Electronic Resource
    Electronic Resource
    β-Turn conformations in crystal structures of model peptides containing α,α-Di-n-propylglycine and α,α-Di-n-butylglycine (1995)
    New York : Wiley-Blackwell
    Biopolymers 35 (1995), S. 1-9 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The crystal state conformations of three peptides containing the α,α-dialkylated residues. α,α-di-n-propylglycine (Dpg) and α,α-di-n-butylglycine (Dbg), have been established by x-ray diffraction. Boc-Ala-Dpg-Alu-OMe (I) and Boc-Ala-Dbg-Ala-OMe (III) adopt distorted type II β-turn conformations with Ala (1) and Dpg/Dbg (2) as the corner residues. In both peptides the conformational angles at the Dxg residue (I: φ = 66.2°, ψ = 19.3°; III: φ = 66.5°. ψ = 21.1°) deviate appreciably from ideal values for the i + 2 residue in a type II β-turn. In both peptides the observed (N…O) distances between the Boc CO and Ala (3) NH groups are far too long (1: 3.44 Å: III: 3.63 Å) for an intramolecular 4 → 1 hydrogen bond. Boc-Ala-Dpg-Ata-NHMe (II) crystallizes with two independent molecules in the asymmetric unit. Both molecules HA and HB adopt consecutive β-turn (type III-III in HA and type III-I in IIB) or incipient 310-helical structures, stabilized by two intramolecular 4 → 1 hydrogen bonds. In all four molecules the bond angle N-Cα-C′ (τ) at the Dxg residues are ≥ 110°. The observation of conformational angles in the helical region of φ,ψ space at these residues is consistent with theoretical predictions. © 1995 John Wiley & Sons, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360350102
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Structure in solution of protected homo-oligopeptides of L-valine, L-isoleucine, and L-phenylalanine: An infrared absorption study (1978)
    New York : Wiley-Blackwell
    Biopolymers 17 (1978), S. 2225-2239 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Monodisperesed, N-and C-Protected homo-oligopeptides [number (n) of resides from 2 to 5] of L-valine, L-isoleucine, and L-phenylalnine were studied by ir absorption spectroscopy between 1200 and 350 cm-1 at various solvents. The solvents and chain-length effects were examined for non-hydrogen-bonded peptide groups. The frequencies of the self-associated species are consistent with a model derived from the amide data. Self-association species are consistent with a model derived from the amide data. Self-association is favored by higher values of n = 2, the peptide is insoluble when more than two chains are bonded. For n = 3, 4, several chains may be associated by sliding along one another and remain soluble. For n = 2, the peptide is insoluble when more than two chains are bonded. For n = 3, 4, several chains may be associated by sliding along one another and remain slouble. For n = 5, the effect of n is to favour a model in which two chains exactly face each other so that the peptide precipitates at relatively low concentration.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1978.360170915
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    Paper (German National Licenses)
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