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The next step is to create or select the package folder. You do this in the dialog box that follows the Printing Instructions form, which on the Mac is called Create Package Folder and in Windows is called Package Publication. In the dialog box, you can select what is copied: the fonts, color-output profiles, and linked graphics (graphics pasted into an InDesign document rather than imported are automatically included). You can also have InDesign update the graphics links for those graphic files that were modified or moved by selecting the Update Graphics Links in Package check box; if this option is not selected, any missing or modified graphics files are not copied with the document. You can tell InDesign to include fonts by selecting the Copy Fonts (Except CJK) check box, to include nonhidden linked graphics by selecting Copy Linked Graphics, and to include linked graphics from hidden layers by selecting Include Fonts and Links from Hidden and Non-Printing Content (which you would do only if you want the service bureau to print those hidden layers or if you were giving the document s files to a colleague to do further work). 8 Working with Text
Both electrophilic and nucleophilic catalysis are exceedingly common components of biocatalytic mechanisms, involving as they do the formation of reactive, metastable covalent intermediates. For instance, metal ions are frequently used by biocatalysts to enhance reaction rates by coordinating to reactive functional groups in substrates and then stabilising those anionic charges formed post-reaction. Other examples of electrophilic catalysis at work in biocatalytic mechanisms involve the covalent use of non-peptidic cofactors that promote enzyme catalysed reaction pathways by acting as electrophilic reactants (electron sinks) that trap substrates covalently in the form of high energy reactive intermediates, which themselves then react before releasing the cofactor for a following round of catalytic activity. Nucleophilic catalysis is also an exceedingly common component of biocatalytic mechanisms. In addition to substrate coordination, metals may also ionise water and in the process provide a source of extremely nucleophilic hydroxyl ions that are considerably more reactive than water. Alternatively, enzyme active sites have a particularly rich source of nucleophilic functional groups donated by such residues as serine, threonine, cysteine, aspartic acid, glutamic acid, lysine, histidine and tyrosine (see 1). These groups all have the propensity to trap appropriate substrates covalently under the right conditions in order to form high energy reactive intermediates, which themselves then react before releasing the functional group for a following round of catalytic activity. ;c l e a r
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Let us now illustrate these methods with some examples. We begin with a self-coupled, real spin-0 field, defined by a Hamiltonian density 3C = Xo + X i n t with [see eq. (2.60) and Lee (1981), $5.61 Un = 4
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