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  • 1975-1979  (2)
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Material
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Year
  • 1
    Electronic Resource
    Electronic Resource
    An investigation of the conformational states of the methylamide of N-acetyl-L-histidine (1977)
    Springer
    Chemistry of natural compounds 12 (1977), S. 323-328 
    Details
    ISSN: 1573-8388
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary 1. All the conformational states of the methylamide of N-acetyl-L-histidine have been calculated. 2. It has been shown that in the case of the tautomer of the imidazole ring with a hydrogen atom on the $${\text{N}}^{\varepsilon _2 }$$ atom, form R of the main chain is preferred, and in the tautomer with the proton on $${\text{N}}^\delta _1$$ and also in the protonated state of the side chain B forms are preferred. 3. The conformational equilibrium is displaced in the direction of form I.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00567808
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Theoretical conformational analysis of N-acetyl-L-leucine methylamide (1976)
    Springer
    Chemistry of natural compounds 11 (1976), S. 217-222 
    Details
    ISSN: 1573-8388
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary 1. A conformational analysis of N-acetyl-L-leucine methylamide has been performed. The interdependence of the conformational states of the main and side chains of the molecule has been investigated. The most suitable orientation of the side chain corresponds to the values of the anglesx 1=x 2=180° and −60°. The overall minimum is located in the B region. 2. The validity of the assignment of leucine to the alanine stereochemical series has been shown. 3. To evaluate the contribution to the stability of the optimum conformations for the entropy of the side chain, conformational maps have been obtained of the statistical sums with a variation at each point of the angles ϕ and ψ of rotation around the Cα-Cγ and Cβ-Cγ bonds from 0 to −160°. 4. The optimum forms of N-acetyl-L-leucine methylamide have been compared with the conformations of leucine residues in proteins. A satisfactory agreement has been obtained between the theoretical and experimental values.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00570671
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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