Residual light

Fig. 13 CORCEMA-ST optimized structure of bovine DHFR/TMP complex. Protein residues within the binding pocket are aqua blue and ligand residues light purple. The hydrogens were omitted for clarity. Reprinted with permission from [75] 2005, American Chemical Society...

A cold, stirred solution of 1-phenyl-piperazine in tetrahydrofuran was treated all at once with [3-(2-methyl-5,6-dimethoxy)indolyl]glyoxalyl chloride. There was an immediate voluminous precipitate of a white crystalline solid which was removed by filtration. The filtrate was taken to dryness and the residual light brown gum was stirred and shaken with water, ethyl acetate and acetic acid. The mixture was warmed on a steam bath and the resulting solid was collected after cooling in an ice bath thus affording l-[(3-(2-methyl-5,6-dimethoxy)indolyl)glyoxalyl]-4-phenylpiperazine as a near white solid, melting point 163°-174°C. 

A solution of l-[(3-(2-methyl-5,6-dimethoxy)indolyl)glyoxalyl]-4-phenyl piperazine in tetrahydrofuran was added over a 10 min period to a stirred suspension of lithium aluminum hydride in tetrahydrofuran. The mixture was refluxed and stirred for 6.5 h and the excess lithium aluminum hydride then destroyed by the dropwise addition of 10% sodium hydroxide solution. The mixture was filtered, the insoluble material was washed with boiling chloroform, and the filtrate dried over anhydrous sodium sulfate and concentrated to dryness. The residual light orange oil was crystallized from a benzene-hexane mixture giving l-[(3-(2-methyl-5,6-dimethoxy)indolyl)ethyl]-4-phenyl piperazine. 

Figure 15.7. Mage desktop window. The desktop window of MAGE program consists of three component windows (graphic window, caption window, and text window) as shown for human lysozyme (1 Iza.pdb, 11zb.pdb, and 11zc.pdb). The displayed structural features can be turned on and off via checkboxes. The check marks (

Fig. 1.9. Kinesin mutant design and single-molecule motility results based on an optical trapping assay, (a) WT full CS. (b) 2G CS with mutated residues (light area in CS). (c) DEL CS is absent. The structure is based on PDB 2K1N, modified to incorporate the Drosophila CS (SwissProt ID P17210). (d) Stall force histogram. Sohd hnes Gaussian fits for WT and 2G a DEL histogram was not fitted because of the unknown number of stalls below the minimum detection force threshold. See [27] for details...

Fig. 1. Domain structure of the Hsp70 and Hsp70-related protein families. Schematic representation of the ATPase domain ( 385 residues, dark gray), a small linker, and the substrate-binding domain, which is subdivided into the /3-sheet ( 150 residues, light gray) and the a-helical subdomains ( 100 residues, gradient). The white boxes in the HspllO and Hspl70 families represent insertions of unknown function.

The emulsification—imbibition of oil into foam, which the lamella number is intended to describe, has been noticed or predicted by a number of authors and was illustrated in Chapter 2. Lobo et al. (50) emphasized the importance of this phenomenon for foam stability. Rater-man (28) predicted that emulsification—imbibition would be important in constant quality preformed foam injection floods. In the core-flood studies of French et al. (54), they observed that the contacting of foam with crude oils produced emulsified droplets of oil within the foam lamellae. Schramm et al. (40) determined MRFs for a number of foams flowing in Berea sandstone cores containing residual light crude oil and found a strong correspondence with the micromodel results (Figure 10). This work was the first to show that foams that are quite stable to oil in the micromodel are also quite effective in core-floods and vice versa. 

---