Region secondary computation

The second type of quantum monodromy occurs in the computed bending-vibrational bands of LiCN/LiNC, in which the role of the isolated critical point is replaced by that of a finite folded region of the spectrum, where the vibrational states of the secondary isomer LiNC interpenetrate those of LiCN [9, 10]. The folded region is finite in this case, because the secondary minimum on the potential surface merges with the transition state as the angular momentum increases. However, the shape of the potential energy surface in HCN prevents any such angular momentum cut-off, so monodromy is forbidden [10]. 

Each protein has a unique three-dimensional shape called its tertiary structure. The tertiary structure is the result of the bends and folds that a polypeptide chain adopts to achieve the most stable structure for the protein. As an analogy, consider the cord in Figure 13-39 that connects a computer to its keyboard. The cord can be pulled out so that it is long and straight this corresponds to its primary structure. The cord has a helical region in its center this is its secondary structure. In addition, the helix may be twisted and folded on top of itself This three-dimensional character of the cord is its tertiary structure. 

The solution of the gas flow and temperature fields in the nearnozzle region (as described in the previous subsection), along with process parameters, thermophysical properties, and atomizer geometry parameters, were used as inputs for this liquid metal breakup model to calculate the liquid film and sheet characteristics, primary and secondary breakup, as well as droplet dynamics and cooling. The trajectories and temperatures of droplets were calculated until the onset of secondary breakup, the onset of solidification, or the attainment of the computational domain boundary. This procedure was repeated for all droplet size classes. Finally, the droplets were numerically sieved and the droplet size distribution was determined. 

Amide III VCD from aqueous solution was published in 1987 [31], and normal coordinate analyses of simple peptides and a number of isotopomers were carried out to define the exact nature of the amide III vibration [32]. Recently, we have reported a detailed comparison of computational and experimental VCD results in the amide I region [33]. Keiderling has pushed the frontiers toward collecting VCD data on a number of proteins, and interpreting the data, via factor analysis, in terms of percentages of the common secondary structures [34,35]. A number of excellent reviews, summarizing the progress in peptide VCD in the 1985-1991 time span, have appeared [36,37],... 

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