Tertiary Comparison Guide Reading Answer
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The Unicode Collation Algorithm is maintained in synchronization with the International Standard, ISO/IEC 14651 [ISO14651]. Although the presentation and text of the two standards are rather distinct, the approach toward the architecture of multi-level collation weighting and string comparison is closely aligned. In particular, the synchronization between the two standards is built around the data tables which define the default (or tailorable) weights. The UCA adds many additional specifications, implementation guidelines, and test cases, over and above the synchronized weight tables. This relationship between the two standards is similar to that maintained between the Unicode Standard and ISO/IEC 10646.
For biomacromolecules, such as proteins and DNAs, we usually know the chirality of the component amino acids or nucleosides and we are more interested in what the CD spectrum tells us about how they are arranged into secondary or even tertiary structures (Figure 3). The use one makes of a CD spectrum depends on what question is being asked: is an absolute measure of helix and sheet content of a protein required? Or does one simply want to know whether a peptide folds in a lipidic environment or a nucleic acid or protein unfolds when heated? The latter questions can often be answered by visual inspection of spectra (Figure 3). However, one does need to take care as to what information is being displayed. In Figure 3c, fluorescence tells us that the tryptophans in α-lactalbumin unfold in two phases, the first being slow and the second from 55oC to 65C. In light of the fluorescence data, the aromatic CD (which is relatively noisy) is probably telling the same story, though it could be one broad transition. By way of contrast, the backbone protein spectrum measured at 222 nm unfolds in a single concerted step from 55oC to 65C, at the same time as the environments of some of the tryptophans is exposed to water as shown by the fluorescence.
An example of batch-to-batch CD comparison of a biopharmaceutical product is given in Figure 5. Visual inspection of the spectra suggests it is largely unfolded (negative maximum at 200 nm), though CD structure-fitting suggests it is β-sheet. The resolution of this, as discussed above, is that it is probably a combination of βII and unfolded structures. Close inspection of the data suggests there is a small difference in the secondary structure of three batches of the product. The aromatic CD suggests the tertiary structures of the different batches also differ.
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