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FIGURE 29.16 The Setup pane of the Print Booklet dialog box
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The Browser tab of the iMovie Preferences window lets you tell iMovie what to do when you click a filmstrip in the Event browser: Show date ranges in Event list. Select this check box if you want iMovie to display the beginning and end date of each Event in the Event Library. Showing the date ranges is helpful when you re working by date as well as by content, but it can make the Event Library appear cluttered. Use large font for project and Event lists. Select this check box if you want the Project Library and Event Library to use a larger font that s easier to read. Always show active clip badges. Clips in Event Browser use project crop setting. Select this check box if you want the Event browser to show clips using the cropping that you ve applied to the project as a whole. Show Fine Tuning controls. If you select this check box, when you point to a clip that you ve already shortened, iMovie displays a button that you can use to change the clip s length.You ll learn how to do this in the next chapter. If you clear this check box, you can pop up the Fine Tuning buttons by pressing +Option while pointing to a clip. Double-click to. Choose the action you prefer to occur when you double-click an event: Edit or Play. Clicking in Events browser deselects all. Select this option button if you find it easier to select by clicking and dragging than by merely clicking.
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at pH 6 and below, in a process mediated via a putative transitional state (intermediate state) (see Figures 4.8 and 4.13 4). The close correlation between binding af nity and conformational data suggested the important conclusion that pH-driven trans-conformational changes are the reason for the changes in binding af nity with pH (conformational pH switch mechanism), implying that only the alkali state of Hsp47 is competent to bind procollagenlike model peptide (PPG)10 and by implication procollagen/collagen. Importantly, the results of all these titration experiments and the conformational pH switch mechanism actually appear to make sense biologically. Hsp47 is known to bind to and assist procollagen assembly in the endoplasmic reticulum (neutral mildly alkali pH) (a major site of protein synthesis is eukaryotic cells) and then remain bound to assist protein traf cking to the cis-Golgi (approximately pH 6.4) (a major site of protein storage before export from eukaryotic cells), where procollagen molecules then dissociate from Hsp47 to begin the process of brilisation prior to export from cells. Hsp47 is then apparently returned to the endoplasmic reticulum in order to repeat the process. Since the conformational pH-switch mechanism is central to the biological activity of Hsp47, further understanding is essential. Detailed site-directed mutagenesis (protein engineering) studies are a powerful way forward (see 3). In the case of Hsp47, histidine amino-acid residues found in histidine clusters (breach, shutter and gate regions) were systematically mutated in turn to alanine residues. Results demonstrated that breach and gate histidines appeared to control and modulate the conformational pH switch, with H191 acting as a potential trigger residue to initiate the correct pH-driven conformational change process (Figure 7.39). Selective mutations of tryptophan residues to phenylalanine residues were then used to determine those sub-domains of Hsp47 most susceptible to conformational change with pH. In the event, the A -sheet region around W100, centred close to H191, was found to be the most in uenced by conformational change as a function of pH (Figure 7.39). Importantly, this region underpins the anticipated binding site region of Hsp47 for collagen/procollagen and procollagen-like model peptide (PPG)10 ! Therefore, the results all seem to interlock to give a complete understanding. So why should a serpin superfamily member become a molecular chaperone involved in procollagen biogenesis In fact, all serpin superfamily members studied to date have a remarkable conformational plasticity. According to the data describe above, this plasticity also seems to be ideally suited to molecular chaperone duties as well!
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balance; rather, it is the amount that accrues when equal payments are made over time to an account that bears a particular rate of interest. Syntax: FV (payment; rate; periods) where payment is the amount of each payment, rate is the interest rate per period, and periods is the number of payment periods. Example: The following expression
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Each of these properties follows the same syntax as the border property, specifying the following properties within its de nition:
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The ability to join paths is new to InDesign CS4.
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Understanding the Flex framework Flash Builder 4 Creating a Flex project Understanding Flex 4
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