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  • Electronic Resource  (3)
  • Polymer and Materials Science  (3)
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  • Electronic Resource  (3)
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  • 1
    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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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Helix-coil stability constants for the naturally occurring amino acids in water. XXIV. Half-cystine parameters from random poly(hydroxybutylglutamine-CO-S-methylthio-L-cysteine) (1990)
    New York : Wiley-Blackwell
    Biopolymers 30 (1990), S. 121-134 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Water-soluble, random copolymers containing N5-(4-hydroxybutyl)-L-glutamine (host) and S-methylthio-L-cysteine (guest) have been prepared, fractionated, and characterized, with S-methylthio-L-cysteine serving as a model for cystine residues in proteins. From the thermally induced helix-coil transition curves of these copolymers in water at neutral pH, the Zimm-Bragg parameters σ and s for the helix-coil transition of “poly(L-cystine)” were deduced. The results show that the cystine model acts as a weak helix-breaker over the entire temperature range from 0 to 60°C. The implications of this finding are evaluated in the context of a general discussion of the Zimm-Bragg parameters for all the 20 naturally occurring amino acids.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360300113
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Helix-coil stability constants for the naturally occurring amino acids in water. XXIII. Proline parameters from random poly(hydroxybutylglutamine-CO-L-proline) (1990)
    New York : Wiley-Blackwell
    Biopolymers 30 (1990), S. 107-120 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Water-soluble random copolymers containing L-proline and N5-(4-hydroxybutyl)-L-glutamine were synthesized by copolymerization of the tripeptides H-L-Glu(OBzl)-L-Glu(OBzl)-L-Glu(OBzl)-OH and H-L-Glu(OBzl)-L-Pro-L-Glu(OBzl)-OH, using ben-zotriazolyl-N-oxy-tris(dimethylamino)-phosphonium hexafluorophosphate as condensing reagent, and subsequent aminolysis of the Bzl ester groups with 4-amino-1-butanol. These copolymers were found to contain significant amounts of N5-(4-hydroxybutyl)-D-glutamine, thus requiring the synthesis of a binary copolymer containing only D- and L-N5-(4-hydroxybutyl)glutamine residues in order to evaluate the possible effects of the D-residues on the conformational properties of poly(hydroxybutylglutamine-co-L-proline). The different copolymers were fractionated, and their thermally induced helix-coil transition curves were obtained in water at neutral pH. When proper corrections were applied for the helix-destabilizing properties of N5-(4-hydroxybutyl)-D-glutamine, the Zimm-Bragg parameters σ and s for L-proline could be deduced from the melting curves of poly (hydroxybutylglutamine-co-L-proline). The results indicate that L-proline acts as a very strong helix breaker over the entire temperature range from 0 to 60°C.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360300112
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    Paper (German National Licenses)
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