Table of proteins

The following table of protein corrections is due to W. M. CiiAEK and H. A. Lubs. They made their comparisons with Clark buffers. 

TABLE 41.3 Lookup Table of Protein Characteristics and Associated PK Behavior... 

Dickerson, R.E. (1979) Chronological Summary Table of Protein Structure Determinations. Private circulation. 

Simulation Studies of Protein-Ligand Interactions 141 Table 2. Table Ligand-protein interaction energies and free energies (kcal/mol). 

A group of 20 ammo acids listed m Table 27 1 regularly appears as the hydrolysis products of proteins All are a ammo acids... 

Table 8. Protein Quality and Digestibility of Nonphotosynthetic Microorganisms...

Plasma fractionation is unusual in pharmaceutical manufacturing because it involves the processing of proteins and the preparation of multiple products from a single feedstock. A wide range of unit operations are utilized to accompHsh these tasks. They are Hsted in Table 3 some are common to a number of products and all must be closely integrated. The overall manufacturing operation can be represented as a set of individual product streams, each based on the processing of an intermediate product derived from a mainstream fractionation process (Fig. 1). 

Much of protein engineering concerns attempts to explore the relationship between protein stmcture and function. Proteins are polymers of amino acids (qv), which have general stmcture +H3N—CHR—COO , where R, the amino acid side chain, determines the unique identity and hence the stmcture and reactivity of the amino acid (Fig. 1, Table 1). Formation of a polypeptide or protein from the constituent amino acids involves the condensation of the amino-nitrogen of one residue to the carboxylate-carbon of another residue to form an amide, also called peptide, bond and water. The linear order in which amino acids are linked in the protein is called the primary stmcture of the protein or, more commonly, the amino acid sequence. Only 20 amino acid stmctures are used commonly in the cellular biosynthesis of proteins (qv). 

Fig. 3. The hierarchy of protein stmctures (a) primary stmcture (see Table 1 for amino acid code) (b) secondary stmcture (c) tertiary stmcture and (d)...

Free substitution of protein meals ia feeds is much more restricted than interchange of oils ia foods. Because of a good balance of essential amino acids, soybean meal is an indispensable ingredient for efficient feeding of nonmminants, eg, poultry and swine. Soybeans provide ca 60% of the world s protein meals, including fish meal (Table 14). Of the 30.0 x 10 t of soybean meal produced in the United States in 1994—1995, 24.2 x 10 t was used domestically, primarily in feeds, and 5.7 x 10 t was exported (50). In the United States, poultry consume the largest share of soybean meal, followed by swine. Lesser amounts are fed to beef and dairy catde. Soybean meal is a principal ingredient in many pet foods (see Feeds and feed additives). 

Wool belongs to a family of proteins, the keratins, that also includes hair and other types of animal protective tissues such as horn, nails, feathers, and the outer skin layers. The relative importance of wool as a textile fiber has declined over the decades as synthetic fibers have increa singly been used in textile consumption. Wool is still an important fiber in the middle and upper price ranges of the textile market. It is also an extremely important export for several nations, notably AustraUa, New Zealand, South Africa, and Argentina and commands a price premium over most other fibers because of its outstanding natural properties of soft handle (the feel of the fabric), moisture absorption abiUties (and hence comfort), and superior drape (the way the fabric hangs) (see Fibers Textiles). Table 2 shows wool production and sheep numbers in the world s principal wool-producing countries. 

Table 14. Effect of Protein and Emulsifier on Coffee Whitener Stability ...

CM Topham, A McLeod, E Eisenmenger, JP Overmgton, MS Johnson, TL Blundell. Erag-ment ranking in modelling of protein structure. Conformationally constrained environmental ammo acid substitution tables. J Mol Biol 229 194-220, 1993. 

The ionic species of the mobile phase will also affect the separation. This is shown in Table 4.3 by the difference in resolution values for magnesium chloride buffer compared to sodium sulfate buffer. In addition, calibration curves for proteins in potassium phosphate buffers are shallower than those generated in sodium phosphate buffers. The slope of the curve in Sorenson buffer (containing both Na and ) is midway between the slopes generated with either cation alone (1). Table 4.4 illustrates the impact of different buffer conditions on mass recovery for six sample proteins. In this case, the mass recovery of proteins (1,4) is higher with sodium or potassium phosphate buffers (pH 6.9) than with Tris-HCl buffers (pH 7.8). 

TABLE 4.2 Comparison of Protein Resolution Factors (Rs) on TSK-GEL SW Columns"... 

TABLE 4.3 Resolution Factors (Rs) of Proteins with Various Ionic Species Added to the Elution Buffer" ... 

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