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Under asynchronous replication, data is stored locally in a log on the master system, pratt, and sent across the network to the destination system, whitney, when network bandwidth or system performance permits Often, depending on the rate of incoming data, data will be replicated just as quickly as it comes in If the rate of incoming data is more than the network or system can handle at that moment, write transactions will stay in the master system s replication log until their turn comes around, when they will be replicated in the order they arrived Writes are confirmed back to pratt s application when they are written to the log on pratt, rather than when they are written to whitney As a result, the impact on pratt s application performance is minimal, and often will approach zero.

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Solved this problem. Modified the data set by populating the values in the same format. Eg., I appended the object as. 123 456 789. and mapped the data-source​ ...

(a) Should the sample mixture be applied to the anodic or the cathodic end of the gel (b) Which of the two proteins will migrate furthest from the origin (c) Migration distances of 9.2 and 2.6 cm were measured for the two standard proteins. An unknown protein migrated 5.2 cm through the same gel after SDS treatment. What is the molecular weight of the unknown protein 3. A mixture of high molecular weight proteins and DNA is separated by agarose gel electrophoresis. Choose a combination of stains from Table 9.1 that would allow the protein bands to be distinguished from the DNA bands on the basis of color. 4. At what approximate pH should a Western blot be conducted, in order to transfer only the proteins in Problem 3 to a nitrocellulose membrane 5. To detect the positions of electrophoretically separated DNA fragments, would ethidium bromide or a biotinylated DNA probe (used in conjunction with an avidin enzyme conjugate and activity stain) be expected to provide positional data for all DNA fragments present in the sample Which would provide selective data for DNA fragments containing a particular sequence

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Figure 3.31. Example of tracking dashboard for translation/transformation ( Axway, 2006)

Since writes under asynchronous replication are read from the log and sent across the network in the same order that they arrived in the log, the data on whitney is always as consistent and usable as it is on pratt at all times, even if it is not perfectly up-to-date Some vendors offer variations on asynchronous replication that do not guarantee write ordering In reality, those variations are periodic replication (see Latency-Based Type 4: Periodic, or Batch-Style, Replication), which does not generally guarantee write ordering on the remote system Unless you are confident that your users and applications can withstand the delays that most synchronous replication solutions introduce, make sure that any replication solution you consider can perform asynchronous replication while maintaining write ordering and data integrity.

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10.1. INTRODUCTION This chapter describes some applications of the principles and methods described in 9. Many variations of zone electrophoresis have been developed as speci c tools for research and diagnostic tests. The examples given in this chapter, while not a comprehensive listing, are representative of the diversity of applications of zone electrophoresis. We will consider the determination of net charge, subunit composition and molecular weight of proteins, the determination of DNA molecular weight, the identi cation of isoenzymes, the diagnosis of genetic disease, DNA ngerprinting, DNA sequencing, and immunoelectrophoresis. 10.2. DETERMINATION OF PROTEIN NET CHARGE AND MOLECULAR WEIGHT USING PAGE1 Using the principles described in 9, multisubunit proteins can be separated according to molecular weight on polyacrylamide gels under nondenaturing conditions. A number of gels are prepared having constant %C and varying %T. The unknown protein and a number of standard proteins of known molecular weight are electrophoresed separately on these gels, with a tracking dye that is not restricted by the gel added to each sample. For each protein on each gel, an Rf value is calculated as the protein migration distance divided by the migration distance of the marker. The Rf values will always lie between zero and unity, provided that the tracking dye has the same charge sign as the protein. When this data has been tabulated, a Ferguson plot of log(Rf) versus %T is constructed for each protein. The net charge ratio (protein:marker) is obtained from the Ferguson plot, as the antilog of the y intercept (%T 0). The negative slope of the Ferguson plot is called KD, and is proportional to molecular weight. A calibration curve of KD versus molecular weight is prepared from data obtained with the protein standards, and the

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