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  • 1995-1999  (2)
  • 1996  (2)
  • Biochemistry and Biotechnology  (2)
  • Retardation analysis  (1)
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  • 1995-1999  (2)
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Keywords
  • 1
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Electrophoresis 17 (1996), S. 12-19 
    ISSN: 0173-0835
    Keywords: Mobility-shift assay ; Retardation analysis ; Nonspecific protein-DNA complexes ; Histone-like bacterial protein ; Cooperative binding ; Gel cage ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The simulated electrophoretic mobility-shift behavior of a model system, in which the nonspecific binding of a protein to a DNA fragment is cooperative, was compared with the experimental behavior of the DNA: histone-like bacterial protein (HU) system. It was concluded that the binding of HU to an 88 bp DNA fragment is, at least, not highly cooperative. The theory of mobility-shift analysis was extended even further to encompass high affinity sequence-specific binding of protein to a DNA fragment followed by weak nonspecific binding, the latter governed by conditional probabilities. In addition to featuring a ladder of incremental protein-DNA complexes, the computed mobility-shift patterns placed emphasis upon stabilization of weak, nonspecific complexes in gel cages.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Electrophoresis 17 (1996), S. 1535-1536 
    ISSN: 0173-0835
    Keywords: Mobility-shift assay ; Nonspecific protein-DNA complexes ; Gel cage ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Theoretical mobility-shift patterns are computed by solution of conservation equations for electrophoresis coupled with chemical reaction. The chemical reaction term is often formulated in terms of dissociation of the protein-DNA complex in a gel cage. This formulation assumes that once the dissociated protein escapes the cage, it goes down a sink and is totally lost. This implies that the concentration of the escaped protein is too low to affect sign ficantly the rates of protein-DNA association along its migration pathway.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
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