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  • Electronic Resource  (2)
  • Amino groups of nucleic acid bases  (1)
  • Key words: Ramachandran map – Protein structure – Molecular modeling – Conformational analysis  (1)
  • 1
    Electronic Resource
    Electronic Resource
    On the relative acidity and basicity of the amino groups of the nucleic acid bases (1978)
    Springer
    Theoretical chemistry accounts 50 (1978), S. 67-73 
    Details
    ISSN: 1432-2234
    Keywords: Amino groups of nucleic acid bases
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Quantum chemical calculations are reported on the deprotonation and protonation of the amino groups of the nucleic acid bases adenine, guanine and cytosine, in an attempt to compare the relative reactivities of these groups. In the light of renewed interest in the amino groups as reactive sites for certain carcinogenic and carcinostatic agents, we discuss the possible significance of our results for the interpretation of these molecular interactions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00552495
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Perspective on “Stereochemistry of polypeptide chain conformations” (2000)
    Springer
    Theoretical chemistry accounts 103 (2000), S. 257-258 
    Details
    ISSN: 1432-2234
    Keywords: Key words: Ramachandran map – Protein structure – Molecular modeling – Conformational analysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract. Despite its apparent simplicity the “Ramachandran map” has been an enormously successful tool for describing and understanding protein structure. Thirty-five years after its invention, it is still used daily for checking the quality of experimental and modeled protein structures. It is, moreover, founded on a rational, reduced-coordinate model of the polypeptide chain which continues to be useful in computational attempts at predicting protein folding.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002149900022
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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