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Protein lysozyme

The presented algorithm was applied to 4 proteins (lysozyme, ribonuclease A, ovomucid and bovine pancreatic trypsin inhibitor) containing 51 titratable residues with experimentally known pKaS [32, 33]. Fig. 2 shows the correlation between the experimental and calculated pKaS. The linear correlation coefficient is r = 0.952 the slope of the line is A = 1.028 and the intercept is B = -0.104. This shows that the overall agreement between the experimental and predicted pKaS is good. [Pg.188]

FIGURE 1.12 Van der Waals packing is enhanced in molecules that are structurally complementary. Gln represents a surface protuberance on the protein lysozyme. This protuberance fits nicely within a pocket (formed by Tyr , Tyr , Phe and Trp ) in the antigen-binding domain of an antibody raised against lysozyme. (See also Figure 1.16.)... [Pg.15]

The model systems, discussed here, contain one type of well-defined protein and one type of well-characterized solid surface in an aqueous medium containing one type of low molecular-weight electrolyte. Table 2 summarizes some relevant properties of the proteins. Lysozyme (LSZ)... [Pg.111]

Addition of the protein lysozyme to DC89PC dispersions resulted in the formation of conical tubules in ethanol-water solution.149 The scanning electron micrograph in Figure 5.37 shows that precipitate from this system is primarily composed of these cones, with a smaller number of cylinders. The cones exhibit more pronounced helical ridges on their exteriors than pure lipid cylinders, suggesting that protein selectively associates to the helical defects in a similar manner as the colloidal particles discussed above. [Pg.331]

Cojocel, C., Dociu, N., Maita, K., Sleight, S.D. and Hook, J.B. (1983). Effects of aminoglycosides on glomerular permeability, tubular reabsorption, and intracellular catabolism of the cationic low molecular weight protein lysozyme. Toxicol. Appl. Pharm. 39 129-139. [Pg.678]

A wide range of reversible adsorption kinetic rates was also found by TIR/FRAP for another protein, lysozyme, on a substrate with a different surface charge, alkylated silicon oxide.(61) It is possible that the wide range of rates results from a spectrum of surface binding site types and/or formation of multilayers of adsorbed protein. [Pg.331]

Proteins (e.g., modified plasma proteins, lysozyme, synthetic peptides, or peptide analogues) [260 - 262] ... [Pg.535]

Kidney Tubular cells Low MW proteins (Lysozyme) Rat, man Nephrotic syndrome Renal cancer... [Pg.373]

Fig. 6 Transition temperature of protein unfolding measured by CE and CD. Proteins lysozyme from chicken egg (LYS), a-lactalbumin from human milk (LAL-h), a-lactalbumin type III from bovine milk (LAL-III), cytochrome c from bovine heart (CYT), recombinant dihydrofolate reductase (DHFR). Fig. 6 Transition temperature of protein unfolding measured by CE and CD. Proteins lysozyme from chicken egg (LYS), a-lactalbumin from human milk (LAL-h), a-lactalbumin type III from bovine milk (LAL-III), cytochrome c from bovine heart (CYT), recombinant dihydrofolate reductase (DHFR).
As with X-ray crystallography, as the molecular weight of the molecule increases, the difficulties in performing structural studies increase. The lanthanide probe method has so far been applied in great detail to only one protein, lysozyme.5 The nuclei studied were protons. Because of the complexity of the protein nmr spectrum, it was necessary to apply techniques to resolve and simplify the spectrum and to assign the observed resonances to specific nuclei in the molecule. Table III lists some details of these methods, with references. [Pg.64]

The overall fold of a globular protein molecule in solution is likely to be given by the X-ray structure of the molecule in a crystal. This has been shown to be the case in detail for one protein, lysozyme, by means of nuclear magnetic resonance techniques, and is highly probable for others. It is necessary, however, to be aware that the conditions under which the protein is crystallized, or studied in solution, can affect the fold, and this has been illustrated with insulin. [Pg.90]

Several types of etched capillaries have been tested with respect to within column reproducibility. For example, the reproducibility of the migration times for 151 consecutive injections of the proteins lysozyme and ribonuclease A was tested on an etched Ci8 modified column at pH = 3.0 [20]. It was found that both solutes gave no discernible increase or decrease in migration time (tM) and its overall reproducibility... [Pg.277]

Mixture of peptides and proteins (lysozyme, angiotensin I and III, bradykinin, ribonuclease A) Cl 8-modified etched capillary 30 mM citric acid-24.5 mM P-alanine, pH 3.0 450 mm x 50 pm i.d. 250 mm effective length 105 ... [Pg.406]

Lewis and Rees1681 determined values of D equal to 2.44, 2.44, and 2.43 for the proteins lysozyme, ribonuclease A, and superoxide dismutase, respectively. Protein regions... [Pg.25]

The following polar amino acid compositions with their internal pK values have been determined for two small proteins, lysozyme and calmodulin. Estimate their isoelectric points. [Pg.84]

Hydrogen-bond partners for internal water molecules. In the five proteins lysozyme, carboxypeptidase, cytochrome c, actinidin and penicillopepsin (Table 19.1), the protein groups (numbers in parentheses) which are bonded to internal water molecules are the main-chain C=0 (75), N-H (38), and side-chain atoms... [Pg.373]

Figure 4 The electrostatic distributions of a-lactalbumin (lALC) (a) and chicken egg-white lysozyme (ILZl) (b) calculated by Delphi and presented by Grasp. Both surfaces of calcium-binding protein a-lactalbumin are mostly negatively charged (a) (in red) while the surfaces of noncalcium binding protein lysozyme (b) are mostly positively charged (in blue)... Figure 4 The electrostatic distributions of a-lactalbumin (lALC) (a) and chicken egg-white lysozyme (ILZl) (b) calculated by Delphi and presented by Grasp. Both surfaces of calcium-binding protein a-lactalbumin are mostly negatively charged (a) (in red) while the surfaces of noncalcium binding protein lysozyme (b) are mostly positively charged (in blue)...
From the difference between the free energy and enthalpy of hydration. The two small globular proteins, lysozyme and ribonuclease, perhaps can be considered compatible at this level of comparison. [Pg.127]

Pfeifer, P. Welz, U. Wippermann, H. Fractal surface dimensions of proteins lysozyme. Chem. Phys. Lett. 1985, 113, 535-540. [Pg.1805]

Nyqvist, H. York, P. Supercritical fluid processing of proteins lysozyme precipitation from aqueous solution. J. [Pg.2581]


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See also in sourсe #XX -- [ Pg.2 , Pg.202 ]

See also in sourсe #XX -- [ Pg.116 ]

See also in sourсe #XX -- [ Pg.107 ]




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