By Verena Beier, Cora Mund, Jörg D. Hoheisel (auth.), Harald Seitz (eds.)
Analytics of Protein-DNA Interactions covers developments in sleek biotechnology. All points of this interdisciplinary expertise, the place wisdom, tools and services are required from chemistry, biochemistry, microbiology, genetics, chemical engineering and desktop technological know-how, are handled. additional info in addition to the digital model is accessible at springer.com.
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Additional resources for Analytics of Protein–DNA Interactions
Using several pairs of oligonucleotides from the human and Galago promoters, harboring these polymorphisms, different protein binding patterns were indeed identiﬁed [6, 16]. , ). Transgenic mouse studies have nevertheless shown that changes in cis-elements are the cause for the evolution of fetal expression: a 4 kilobase fragment of the human γ -globin was highly expressed in mouse fetal liver, whereas the comparable fragment from the Galago γ -globin gene was expressed selectively in embryonic life .
4a). Nonlinearity of the ln d(R) dt = f (t) plot suggests that the interaction cannot be analyzed using a 1 : 1 model or that other processes, such as mass transport (Sect. 3), interfere with DNA · PROTEIN complex formation. Besides being an important diagnostic plot, the ln d(R) dt = f (t) function can also be used for evaluation of the DNA · PROTEIN complex formation rate constant kon . The plot kobs vs C is linear (Eq. 2) and the slope of this function represents the kon rate constant (Fig. 4b).
7 for sequential binding and sequential binding followed by a conformational change model, respectively. Authors of the study found that these two models give the best description of the interaction. 5 Qualitative Analysis The major application of SPR methods in studying DNA–protein binding is extracting the kinetic parameters of an interaction. However, qualitative analysis of the sensorgram can also provide useful information. 1 Stoichiometry Determination The response measured in SPR experiments is not only proportional to the amount of protein–DNA bound to a chip surface (a prerequisite of kinetic analysis), but also the change in the bulk refractive index per unit change in protein concentration (speciﬁc refractive index increment) is closely similar for a wide range of proteins and nucleic acids.