Creamer

Coffeeberry Coffee cake Coffee (Continued) Coffee creamers Coffee grounds... 

Products prepared from soy protein products and resembling chicken, ham, frankfurters, and bacon are available commercially. Soy protein isolates are used in place of milk proteins or sodium caseinate in products such as coffee creamers, whipped toppings, yogurt, and infant formulas (see Dairy substitutes). Soy protein products also are used in snacks and in baked foods. 

Aurora, R., Creamer, T, Srinivasan, R., and Rose, G. D., 1997. Local interactions in protein folding Lessons from die ci-helix. TheJournal of Biological Chemistry 272 1413-1416. 

Ms. Abramson s pride and joy is the Kentucky Turban. It is bourbon and chai, the Indian spice milk tea, with coconut milk as a creamer. 

In addition to their nutrient value, casein proteins have many other uses. They are good emulsifiers, helping fats to stay suspended in water-based products such as milkshakes, coffee creamers, and ice creams. They are used as binders in processed meats (lunch meats, sausages, etc.). 

Gezimati, J., Creamer, L. K., and Singh, H. (1997). Heat-induced interactions and gelation of mixtures of p-lactoglobulin and a-lactalbumin. /. Agric. Food Chem. 45,1130-1136. 

Three theory papers are also included. Determinants of the Polyproline II Helix from Modeling Studies by Creamer and Campbell reexamines and extends an earlier hypothesis about Pn and its determinants. Hydration Theory for Molecular Biophysics by Paulaitis and Pratt discusses the crucial role of water in both folded and unfolded proteins. Unfolded State of Peptides by Daura et al. focuses on the unfolded state of peptides studied primarily by molecular dynamics. 

A model of a Pn helix formed by alanine side chains is illustrated for reference in Figure 13B (see color insert), while Figure 13A illustrates the common occurrence of the Pn backbone conformation among residues outside regions of regular secondary structure (Kleywegt and Jones, 1996 Serrano, 1995 Stapley and Creamer, 1999) in protein structures from the Protein Data Bank. 

Fig. 16. CD spectra of the K7 (black spectrum) and P7 (gray spectrum) peptides in pH 7 solutions at 20°C. From Rucker and Creamer (2002). Protein Sri. 11,980-985, 2002, Reprinted with permission from the Protein Society.

RWW thanks Ms. Janice Chapman and Dr. Narasimha Sreerama for their expert assistance. ZS and NRK thank Drs. Robert L. Baldwin, Trevor Creamer, Tobin Sosnick, Michael Levitt and George Rose for helpful discussions and guidance. Preparation of this manuscript and the research described herein from the Woody and Kallenbach laboratories, published and unpublished, have been supported by NIH Grant GM 22994 (RWW) and ONRgrantN00014-02-1-0125 (NRK). 

A common approach in the study of secondary structure or small pieces of structure is to survey known protein structures for all instances of such structures and then to analyze those found. Such an approach has been taken for PPII helices (Adzhubei and Sternberg, 1993 Stapley and Creamer, 1999) and for residues that adopt the PPII conformation but are not necessarily part of PPII helices (Sreerama and Woody,... 

The PPII conformation is abundant in known protein structures, although PPII helices are not particularly common. Sreerama and Woody (1994) found that around 10% of all protein residues are in the PPII helical conformation. However, the majority of those are not part of a PPII helix. Stapley and Creamer (1999) and Adzhubei and Sternberg (1993) found that only 2% of the residues in the proteins examined were part of PPII helices four residues or longer in length. Moreover, on average, each protein possesses just one such PPII helix. The PPII helices found tend to be very short. Stapley and Creamer (1999) found that 95% of the PPII helices in their protein data set were only four, five, or six residues long. 

Fig. 2. Plot of %PPII content (Kelly et al., 2001 A. L. Rucker, M. N. Campbell, and T. P. Creamer, unpublished results) against Chou-Fasman frequency to be in a PPII helix, Pppii (Stapley and Creamer, 1999).

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