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The basic structural information available from intrinsic uorescence spectroscopy of biological macromolecule structures is quite limited compared with information available from even UV visible or even CD spectroscopy and is largely limited to globular proteins. One of the main reasons for this is that only proteins and nucleic acids possess substantial numbers of chromophores that are potentially capable of absorbing photons leading to uorescence emission. However, not every chromophore is simultaneously a good uorophore (i.e. chromophore capable of generating uorescence emission). Indeed, the nucleic acid bases are fundamentally poor uorophores. In proteins, only tryptophan amino-acid residues are substantial uorophores out of the three main aromatic amino-acid chromophores. Moreover, values of F are low in water, though values of R are short, hence generally limiting uorescence utility even further (Table 4.1). In spite of these limitations, uorescence spectroscopy of proteins involving intrinsic tryptophan residue uorescence (excitation 295 nm) can be a useful monitor of conformational changes in globular proteins in a way similar to UV visible spectroscopy of tryptophan residues in globular proteins. If the local environment of a tryptophan residue is changed from hydrophilic (or polar) to hydrophobic, then this leads to an increase in uorescence emission ( * ) transition energies associated with a decrease in transition wavelength (blue-shift) (typically 350 330 nm). Since the interior of such a protein may be regarded as hydrophobic whilst the exterior is hydrophilic, then we can generalise to say that interior buried residues are blue-shifted compared with solvent-exposed residues. Furthermore, interior buried residues will not be subject to internal conversion problems caused by random collisions with water molecules, or to collisional deactivation with quenching molecules. Therefore, values of F should increase substantially according to Equation (4.21), resulting in signi cantly enhanced uorescence emission intensities. Both characteristics ensure that

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d a t a <= HEX2LED_ROM(to_integer(unsigned(addr))); end a r c h ;

Those are shown in Table 13-10 along with estimates of the ranges of variables for the various regimes [similar to those of Doraiswamy and Sharma (1984)] and important variables for design and scale-up Levenspiel (1999) has estimated the effect of liquid-phase chemical reaction on the mass transfer coef cient, kL The modi ed coef cient is given here as k L For Middleton s regime V, where the chemical reaction is so fast that the reaction front is within the mass transfer lm, the modi ed mass transfer coef cient for the gas phase component of the reaction is k = kL 1 + L DAL CA DBL C B (13-25).

With a studio setup at home, the lighting is controlled and the exposure is fairly constant. To work faster and more consistently, professional photographers use either a light meter or a gray card (see Figure 23-12). Both provide good, accurate exposure. A light meter is more expensive than the gray card and provides a bit more data. But a gray card is inexpensive and is sufficient for most of your home studio needs. Pick one up at a photography store for about $15. It will give you the correct exposure every time.

1. Open the destination database file in FileMaker Pro and switch to Browse mode. 2. Optional: If you intend to replace or update records in the current database with imported records, you can use Find commands to select the records to be replaced or updated. (This assumes that you do not wish to replace or update all records in the database.) 3. Choose File Import Records File. The Open File dialog, as shown in Figure 16-6, appears. At the bottom of the dialog is a Show pop-up menu /Files of type drop-down list where you can select the format of the file that you want to import.

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