Protein flow time behavior

Finally, a summary of the flow time behavior of protein adsorption from the 1 1 albumin-fibrinogen solution is listed ... 

However, by examining the adsorption behavior of polypeptides and proteins with comparable porous and nonporous particles in finite baths, packed columns and expanded or fluidized beds, an iterative simulation approach based on the heuristic principles described earlier and along the lines of the flow diagram shown in Fig. 32 can be developed, leading ultimately to the implementation of useful scale-up criteria. Along the way, computer simulations, generated from the analysis of the concentration-time... 

Proteins in solution are also sensitive to orthokinetic aggregation, i.e., shear-induced aggregation. We have observed this phenemenon at very low shear rates in the case of BSA, ovalbumin, and BLG [28,29] in Fig. 1, one sees that the viscosity of the protein solution increases with time till it reaches a plateau the phenomenon becomes less and less pronounced as the shear rate increases, so much so that the solution displays time-independent and Newtonian flow behavior in the usual shear rate range. 

As indicated earlier, we initially studied the adsorption of proteins from flowing aqueous solutions of single proteins, which allowed us to establish a baseline for the time-adsorption behavior of each of the proteins. The protein buildup was monitored as the adsorbed layer increases in thickness. An example of this is shown in the spectra of Figure 9 which show how the protein layer adsorbed from an albumin solution changes with time. In addition to an increase in the amount of adsorbed protein, changes with time occur in the 1300-cm 1 region of the Amide III complex. The adsorbed... 

In order to stndy the short time vibrational energy transfer behavior of a vibra-tionally excited system, we employ a non-Markovian time-dependent perturbation theory [83]. Onr approach builds on the successful application of Markovian time-dependent pertnrbation theory by Leitner and coworkers to explore heat flow in proteins and glasses, and Tokmakoff, Payer, and others, in modeling vibrational population relaxation of selected modes in larger molecules. In a separate chapter in this volnme, Leitner provides an overview of the development of normal mode-based methods, snch as the one employed here, for the study of energy flow in solids and larger molecnlar systems. 

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