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Lysozyme nature

Figure 2. (a) The amino acid sequence of the enzyme lysozyme (from egg white). Blocks enclosing two cysteines (Cys) denote intramolecular covalent cross-links (disulfide bonds). This molecule in crystalline form has the three-dimensional structure sketched in part (b). Note the helical subdomains and sheet substructures formed by nearby extended segments. Reprinted by permission from C. C. F. Blake, Structure of Hen Egg-White Lysozyme, Nature vol. 206 p. 757. Copyright (c) 1967 Macmillan Magazines Ltd. [Pg.434]

Alber T, Dao-pin S, Wilson K, Wozniak JA, Cook SP, Matthews BW (1987) Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. Nature (Lond) 330 41-46... [Pg.536]

Blake CCF, Fenn RH, North ACT, Phillips DC, Poljak RJ (1962) Structure of lysozyme. Nature 196 1173-1176... [Pg.118]

S. E. Radford and C. M. Dobson. From computer simulations to human disease emerging themes in protein folding. Cell, 97 (1999), 291 M. Bucciantini, E. Giannoni, F. Chiti et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature, 416 (2002), 507 M. Dumoulin, A. M. Last, A. Desmyter et al. A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme. Nature, 424 (2003), 783 F. Chiti, M.Stefani,... [Pg.254]

Lysozyme. — Natural abundance n.m.r. spectroscopic studies have been reported for native lysozyme, lysozyme in solution with Gd ", La, Eu, Pr ", and Co, and lysozyme modified by treatment with iodine at pH 5.5. It was possible in the case of the chemically modified enzyme to assign certain resonances to specific residues in the molecule. [Pg.674]

Grutter, M.G., L.H. Weaver, and B.W. Mattews. 1983. Goose lysozyme structure An evolutionary link between hen and bacteriophage lysozyme. Nature 303 828-831. [Pg.375]

Demotz, S., Grey, H., Appeiia, E., and Sette, A. (1989) Characterization of a naturally processed MHC class II restricted T-cell determinant of hen egg lysozyme. Nature 342, 682-684. [Pg.388]

E. P. Abraham, Some Properties of Egg-White Lysozyme, Biochem.. 33,622-630 (1939). E.P. Abraham and R. Robinson, Crystallization of Lysozyme, Nature, Lond. 140, 24 (1937). [Pg.365]

M.R. J. Salton, Cell Wall of Micrococcus lysodeikticus as the Substrate of Lysozyme, Nature, Lond. 170, 746-747 (1952). [Pg.387]

Salser, W., Gesteland, R. F., Bolle, A. In vitro synthesis of bacteriophage lysozyme. Nature (Lond.) 215, 588-591 (1967). [Pg.128]

FIR Faber, BW Matthews. A mutant T4 lysozyme displays five different crystal conformations. Nature 348 263-266, 1990. [Pg.310]

M Totrov, R Abagyan. Detailed ah initio prediction of lysozyme-antibody complex with 1.6 AA accuracy. Nature Struct Biol 1 259-263, 1994. [Pg.311]

Figure 17.4 Melting temperatures, Tm, of engineered single-, double-, and tripledisulfide-containing mutants of T4 lysozyme relative to wild-type lysozyme. The red bars show the differences in Tm values of the oxidized and reduced forms of the mutant lysozymes. The green bars for the multiple-bridged proteins correspond to the sum of the differences in Tm values for the constituent single-bridged lysozymes. (Adapted from M. Matsumura et al.. Nature 342 291-293, 1989.)... Figure 17.4 Melting temperatures, Tm, of engineered single-, double-, and tripledisulfide-containing mutants of T4 lysozyme relative to wild-type lysozyme. The red bars show the differences in Tm values of the oxidized and reduced forms of the mutant lysozymes. The green bars for the multiple-bridged proteins correspond to the sum of the differences in Tm values for the constituent single-bridged lysozymes. (Adapted from M. Matsumura et al.. Nature 342 291-293, 1989.)...
Figure 17.5 Diagram of the T4 lysozyme stmcture showing the iocations of two mutations that stabilize the protein stmcture by providing eiectrostatic interactions with the dipoles of a helices. (Adapted from H. Nicholson et al.. Nature 336 651-656, 1988.)... Figure 17.5 Diagram of the T4 lysozyme stmcture showing the iocations of two mutations that stabilize the protein stmcture by providing eiectrostatic interactions with the dipoles of a helices. (Adapted from H. Nicholson et al.. Nature 336 651-656, 1988.)...
In order to make an effective use of the VB formulation we have to calibrate the relevant parameters using reliable experimental information. The most important task is to obtain the relevant a-. Since the a s represent the energy of forming the different configurations in the gas phase at infinite separation between the given fragments, it is natural to try to obtain them from gas-phase experiments. In the case of the catalytic reaction of lysozyme one can compile the relevant information from the available gas-phase experiments (Table 6.1) and use it to determine the a s. [Pg.162]

Blake CC, Koeniz DF, Mair GA, North AC, Phillips DC, Sarma VR. Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution. Nature 1965 206 757-61. [Pg.298]

Aldrich, J.E., Cundall, RB., Adams, G.E. and Willson, RL. (1969). Identification of essential residues in lysozyme a pulse radiolysis method. Nature 221, 1049-1051. [Pg.19]

Research is under way to investigate the potential to develop the natural antimicrobial system present in milk, such as the lysozyme, lactoferrin,... [Pg.104]

The effect of pH on the protein adsorption on CMK-3 was also investigated [152], The monolayer adsorption capacities obtained under various pH conditions are plotted in Figure 4.12, where the maximum adsorption was observed in the pH region near the isoelectric point of lysozyme (pi of about 11). Near the isoelectric point, the net charges of the lysozyme molecule are minimized and would form the most compact assembly. A similar pH effect was also seen in the adsorption of cytochrome c on CM K-3. Although the nature of the surface of mesoporous silica and... [Pg.127]

Concerning the nature and structure of such amyloid peptide or protein channels, oligomers with annular morphologies have in fact been observed by EM for a-synuclein (Lashuel et al., 2002) and equine lysozyme (Malisauskas et al., 2003) even in the absence of any lipids or membranes. Channel-like structures have also been reconstituted in liposomes and observed by SFM for A/ i 4o, A/ j 42, human amylin, a-synuclein, ABri, ADan, and serum amyloid A (Fig. 5A Lin et al., 2001 Quist et al., 2005). Doughnut-shaped structures with a diameter of 10-12 nm and a central hole size of 1-2 nm (Fig. 5B) were imaged on top of lipid membranes (Quist et al., 2005). However, the radius of curvature of the SFM tips meant that it is not possible to say whether the pores were really traversing the lipid bilayer. [Pg.227]

Starch (1), Cellulose (2), Cellulose Methyl Ether (3), Oxy-cellulose (4), PVA (5), Partially Hydrolyzed PVAc (6), Silk (.2), Wool (7), Hide-Powder (8), Natural Rubber Latex ( ), Synthesized Poly-(ot-Amino Acids) (10), Nylon-6 (11), Nylon-3 (12), Ot-Amylase (13), Lysozyme (14), RNA (15), Polyacrylonitrile (16), Polyvinyl-sulfonate (17) ... [Pg.103]


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Lysozyme

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