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  • 1
    Electronic Resource
    Electronic Resource
    A computergraphic determination of the chemotactic peptide preferred conformation
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 157 (1988), S. 569-574 
    Details
    ISSN: 0006-291X
    Keywords: [abr] Acc; aminocyclohexanecarboxylic acid ; [abr] Aib; alpha-aminoisobutyric acid ; [abr] Boc; N-^tbutyloxycarbonyl ; [abr] FMLP; N-formylmethionyl-leucyl-phenylalanine ; [abr] For; N-formyl
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0006-291X(88)80287-0
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  • 2
    Electronic Resource
    Electronic Resource
    A computergraphic determination of the chemotactic peptide preferred conformation
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 157 (1988), S. 569-574 
    Details
    ISSN: 0006-291X
    Keywords: [abr] Acc; aminocyclohexanecarboxylic acid ; [abr] Aib; alpha-aminoisobutyric acid ; [abr] Boc; N-^tbutyloxycarbonyl ; [abr] FMLP; N-formylmethionyl-leucyl-phenylalanine ; [abr] For; N-formyl
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0006-291X(88)80287-0
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Sequence-Dependence of secondary structure formation: Conformational studies of host-guest peptides in α-helix and β-structure supporting media (1985)
    New York : Wiley-Blackwell
    Biopolymers 24 (1985), S. 1057-1074 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A newly designed host-guest approach is introduced as a experimental tool to explore the relationship between the sequence of peptides and their secondary structure. From the CD spectra of the host-guest peptides studied, a tentative scale for the α-helix potential in 2,2,2-trifluorethanol of guest amino acids is delineated. The conformational preferences are also examined in β-structure supporting media (solid state, CH2Cl2, CH3OH, H2O) using ir-absorption and CD techniques. Scales for the β-forming tendency of guest amino acid residues in the different media are delineated. It is shown that the preferred conformation of the host-guest peptides is a function of the medium, the chain length, and the protecting groups. Given the fact that conformational effects are important in peptide synthesis, the tentative scales may serve as a guideline to predict secondary structures of side-chain-protected or -deprotected peptides in a given solvent, complementing the well-known empirical conformational prediction parameters.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360240610
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  • 4
    Electronic Resource
    Electronic Resource
    Vibrational circular dichroism of polypeptides. IV. Film studies of L-alanine homo-oligopeptides (1985)
    New York : Wiley-Blackwell
    Biopolymers 24 (1985), S. 1257-1263 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Vibrational CD (VCD) and ir absorption data are reported for a series of films of Boc-(L-Ala)n-OMe homo-oligopeptides (n = 3-7) in the amide I and A regions. The data evidenced a sharp change between n = 3 and n = 4, which parallels the onset of β-structure formation, and another between n = 5 and n = 6, which parallels the full development of β-structure. This represents the first report of the application of VCD to oligopeptide conformation. The data resembled earlier reported film VCD studies of higher-molecular-weight polypeptides of known β-structure.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360240712
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  • 5
    Electronic Resource
    Electronic Resource
    Stereochemistry of peptides containing 1-aminocyclopentanecarboxylic acid (Acc5): Solution and solid-state conformations of Boc-Acc5-Acc5-NHMe (1986)
    New York : Wiley-Blackwell
    Biopolymers 25 (1986), S. 1635-1644 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The conformational analysis of a protected homodipeptide of 1-aminocyclopentanecarboxylic acid (Acc5) has been carried out. 1H-nmr studies establish a β-turn conformation for Boc-Acc5-Acc5-NHMe in chloroform and dimethylsulfoxide solutions involving the methylamide NH in an intramolecular hydrogen bond. Supportive evidence for the formation of an intramolecular hydrogen bond is obtained from ir studies. X-ray diffraction studies reveal a type III β-turn conformation in the solid state stabilized by a 4 → 1 hydrogen bond between the Boc CO and methylamide NH groups. The φ,ψ values for both Acc5 residues are close to those expected for an ideal 310-helical conformation (φ≃ ± 60°, ψ∼ ±30°).
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360250907
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  • 6
    Electronic Resource
    Electronic Resource
    Structural versatility of peptides from Cα,αdialkylated glycines: Linear Ac3c homo-oligopeptides (1989)
    New York : Wiley-Blackwell
    Biopolymers 28 (1989), S. 175-184 
    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 molecular structures of five linear Ac3c homo-oligopeptides to the tetramer were determined by x-ray diffraction. The oligomers are H-(Ac3c)2-OMe, Fmoc-(Ac3c)2-OMe MeOH, Ac-(Ac3c)2-OMe, pBrBz-(Ac3c)3-OMe · H2O, and t-Boc-(Ac3c)4-OMe · 2H2O. The results indicate the propensity of the tri- and tetrapeptides to fold into type I β-bends and distorted 310-helices, respectively, in partial contrast to Aib, Ac5c, and Ac6c homo-peptides of comparable main-chain length, where regular type III β-bends and 310-helical structures were found. When the influence of the constraints produced by the intramolecular H bonds of the C10-type is absent, other less common structural features may be observed. The average geometry of the cyclopropyl group of the Ac3c residue is found to be asymmetric and the N—Cα—C′ bond angle significantly expanded from the regular tetrahedral value.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360280119
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  • 7
    Electronic Resource
    Electronic Resource
    Preferred conformation of peptides from Cα,α-symmetrically disubstituted glycines: Aromatic residues (1991)
    New York : Wiley-Blackwell
    Biopolymers 31 (1991), S. 637-641 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The conformational preference of Cα,α-diphenylglycinc (Døg) and Cα,α-dibenzylglycine (Dbz) residues was assessed in selected derivatives and small peptides by conformational energy computations, ir absorption, 1H-nmr, and x-ray diffraction. Conformational energy computations on the two monopeptides strongly support the view that these Cα,α-symmetrically disubstituted glycines are conformationally restricted and that their minimum energy conformation falls in the fully extended (C5) region. The results of the theoretical analyses appear to be in agreement with the solution and crystal-state structural propensities of three derivatives and seven di-and tripeptides.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360310608
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  • 8
    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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  • 9
    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)
  • 10
    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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