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The first instruction performs normal addition of the least significant bytes and stores the carry-out bit into the carry flag. The second instruction then includes the carry flag when adding the middle bytes. Similarly, the third instruction uses the carry flag from the previous addition to obtain the result for the most significant bytes. The incrementing and subtraction of multiple bytes can be achieved in a similar fashion:

Note that the memory row is defined in ascending order:



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If you append the following line of code to the preceding, you can see that by setting the tabIndex property for tComments, tComments is included in the sequence:





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If this prospect is realised, then it is expected that many of the advances to ow from the Grid will come from applications that can combine information from multiple data sets This will allow researchers to combine different types of information on a single entity to gain a more complete picture and to aggregate the same types of information about different entities Achieving this will require support for integrating data from multiple DBS, for example, through distributed query and transaction facilities This has been an active research area for several decades, and needs to be addressed on multiple levels As was the case for metadata-driven access, the design of federation middleware will be made much more straightforward if DBS can be accessed through standard interfaces that hide as much of their heterogeneity as possible.

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Mass spectrometry is a technique with origins in the physical sciences that has fast become one of the most powerful techniques available for probing biological systems. Advances in mass spectrometry made possible by the advent of soft ionisation techniques have made possible detailed investigations into the primary structures of biological macromolecules and amphiphilic lipids. Indeed, mass spectrometry could be seen as the pre-eminent technique for determining the primary structures of polypeptides, nucleic acids, and complex carbohydrates owing to the possibility of obtaining molecular mass and sequence information using minute quantities of material (femtomole picomole, even attomole levels). Such information can be obtained without even the need for recombinant technologies (see 3). Hence, although three-dimensional information is not directly available by mass spectrometry, impressive amounts of primary structural information are nevertheless available that can be integrated with other pieces of information to try and provide useful insights into biological macromolecular structure without the need for analyses of the type presented in s 5 and 6. However, nowadays, mass spectrometry is also known to be essentially indispensable to the eld of proteomics, de ned as the study of all the interactions and implied functions of all the proteins expressed from a genome. Chemical biology and multidisciplinary thinking have very much driven the development of proteomics from the development of suitable mass spectrometric methods for large scale protein identi cation, to the development of suitable chromatographic systems to map out protein networks (Figure 9.1). In other words, mass spectrometry not only gives us primary structures but also has the capacity to de ne complex, functional, three-dimensional networks of interacting proteins and polypeptides within cells. Mass spectrometry quite simply lifts us from the opportunity to make detailed investigations into the structures and functions of certain biological macromolecules of interest

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