Deletional joining

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You can now see why for line A a branch-and-bound technique is not required to solve the design problem. Because of the way the objective function is formulated, if the ratio (pd ps) = 1, the term involving compressor i vanishes from the first summation in the objective function. This outcome is equivalent to the deletion of compressor i in the execution of a branch-and-bound strategy. (Of course the pipeline segments joined at node i may be of different diameters.) But when... 

Hesse, J.E., Lieber, M.R., Gellert, M., Mizuuchi, K. (1987). Extrachromosomal DNA substrates in pre-B cells undergo inversion or deletion at immunoglobulin V-(D)-J joining signals. Cell 49,... 

The assembly of polypeptide chains into functional fibrinogen molecules has been studied in several expression systems. The order in which the polypeptide chains are joined together by disulfide bonds has been determined and specific structural features that are important for assembly, such as the coiled-coil, have been identified (Xu et al., 1996). Substitution of the cysteines with serine showed that the interchain disulfide ring at the proximal end of the coiled-coil, in addition to the disulfides between the two halves of the molecule, are necessary for assembly of the two half molecules (Zhang and Redman, 1996). The distal interchain disulfide ring is not necessary for assembly of the two half molecules but is necessary for secretion. Disruption of intrachain disulfide bonds and deletions of portions of the polypeptide chains have revealed which... 

The above procedure ends when an isolated vertex is created or when all vertices of H are pairwise deleted. In the former case H is non-Kekulean in the latter case it is Kekulean, and a Kekule structure can be constructed by regarding the edge joining the deleted pair of vertices at each step as a double bond. 

As noted above, the two lobes have very similar folding. This is only to be expected given their high (—40%) sequence identity. The differences, at the level of polypeptide folding, are confined primarily to small insertions and deletions in the loops that join secondary structure elements. These are almost all located on the molecular surface and do not disturb the basic structure—indeed 90% of the main chain atoms of the N-lobe of human lactoferrin can be superimposed on equivalent atoms in the C-lobe with a root-mean-square deviation of only —1.2 A. The agreement would be even closer were it not for the small difference in the closure of the two domains, described above. 

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