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  • 1
    Electronic Resource
    Electronic Resource
    Ab-initio molecular orbital studies on a new mechanism for the interconversion of monomethylnitrosamine and methyldiazohydroxide (1986)
    Springer
    Theoretical chemistry accounts 70 (1986), S. 421-427 
    Details
    ISSN: 1432-2234
    Keywords: Molecular orbital ; Nitrosamine metabolism ; Monomethyl nitrosamine ; Methyldiazohydroxide ; Mechanism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Monomethylnitrosamine and methyldiazohydroxide are two proposed N-nitrosamine metabolites, which are formally related by an N → O 1,3-proton shift. Their possible interconversion is an important reaction to investigate in elucidating the pathways involved in the decomposition of carcinogenic N-nitrosamines. Self-consistent field molecular orbital studies using a 4-21G basis set, in which solvation is treated using the supermolcule approach, have led to the proposal of a new low energy pathway for their interconversion; this mechanism involves protonation and the implicit involvement of at least two molecules of water.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00531923
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Inclusion of conserved buried water molecules in the model structure of rat submaxillary kallikrein (1997)
    Springer
    Journal of computer aided molecular design 11 (1997), S. 547-556 
    Details
    ISSN: 1573-4951
    Keywords: Molecular modelling ; Protein structure ; Rat submandibular kallikrein ; Molecular dynamics ; Homology modelling
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A new approach to the molecular modelling of homologous serine proteases isadopted, by including a set of 21 buried waters known to be preserved inenzymes sharing the primary specificity of trypsin, in the homology modellingof rat submaxillary gland kallikrein. Buried waters – water moleculessequestered from bulk solvent within a protein matrix – appear to beintegral conserved components of all serine proteases of known structure andshould be incorporated into serine protease models built on the basis ofsequence/structural homology to this family. The absence of such waters mightinduce errors in a force field simulation, favouring the formation ofnonexistent hydrogen bonds and locally inaccurate structure. The kallikreinmodel refinement has led to the conclusion that an additional buried watershould be added to the original rigid matrix of 21 conserved water molecules.The structurally preserved protein cavities of such waters validate themodelled structure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007919812771
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    Paper (German National Licenses)
    Fulltext
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