Hen lysozyme

Here, two different sequences from transth3Tetin were successfully combined into mixed fibrils [54], This is not always the case, however. For amyloidogenic proteins, the ability of other fibrils to act as cross-seeds for growth is known to depend on sequence similarity [55]. Seeding hen lysozyme solutions with seeds formed from closely related sequences (e.g. hen and other lysozymes) led to the largest increases in the rate of formation of fibrils. Consequently, there may be some restrictions on the selection of distinct peptide sequences to produce scaffolds. 

Yang JJ, Pitkeathly M, Radford SE (1994) Far-uv circular-dichroism reveals a conformational switch in a peptide fragment Irom the beta-sheet of hen lysozyme. Biochemistry 33 7345-7353... 

The ROA spectra of partially unfolded denatured hen lysozyme and bovine ribonuclease A, prepared by reducing all the disulfide bonds and keeping the sample at low pH, together with the ROA spectra of the corresponding native proteins, are displayed in Figure 5. As pointed out in Section II,B, the short time scale of the Raman scattering event means that the ROA spectrum of a disordered system is a superposition of snapshot ROA spectra from all the distinct conformations present at equilibrium. Because of the reduced ROA intensities and large... 

Fig. 5. Backscattered Raman and ROA spectra of native (top pair) and reduced (second pair) hen lysozyme, and of native (third pair) and reduced (bottom pair) bovine ri-bonuclease A, together with MOLSCRIPT diagrams of the crystal structures (PDB codes llse and lrbx) showing the native disulfide links. The native proteins were in acetate buffer at pH 5.4 and the reduced proteins in citrate buffer at pH 2.4. The spectra were recorded at 20°C. 

The ROA spectra of native and prehbrillar amyloidogenic human lysozyme are displayed in Figure 7, together with a MOLSCRIPT diagram of the native structure. The ROA spectrum of the native protein is very similar to that of hen lysozyme (Fig. 5). However, large changes have occurred in the ROA spectrum of the prehbrillar intermediate. In particular, the positive 1340 cm-1 ROA band assigned to hydrated... 

Kunichika, K., Hashimoto, Y. and Imoto, T. (2002) Robustness of hen lysozyme monitored by random mutations. Protein Engineering, 15, 805-809. 

Kamatari YO, Konno T, Kataoka M, et al. The methanol-induced transition and the expanded helical conformation in hen lysozyme. Protein Sci. 1998 7 681-688. 

D. Horsley, J. Herron, V. Hlady, and J. D. Andrade, Human and hen lysozyme adsorption A comparative study using total internal reflection fluorescence spectroscopy and molecular graphics, in Proteins at Interfaces Physicochemical and Biochemical Studies (J. L. Brash and T. A. Horbett, eds.), ACS Symposium Series No. 343, pp. 290-305, American Chemical Society, Washington, D.C. (1987). 

Fig. 1. Representation of the active site region of hen lysozyme, from the X-ray structure (adapted from Ref. 31). The lanthanide cations bind in the region between asp 52 and glu 35.

Figure 3-2 Acid-base titration curve for hen lysozyme at 0.1 ionic strength and 25°C. O, initial titration from the pH attained after dialysis , hack titration after exposure to pH 1.8 A, hack titration after exposure to pH 11.1. The solid curve was constructed on the basis of "intrinsic" pKa values based on NMR data. From Kuramitsu and Hamaguchi5...

Figure 3-28 A15N - H HSQC spectrum of partially denatured 129-residue hen lysozyme. Boxes enclose the tryptophan indole region (upper left), the arginine side chain NE region (upper left), and a portion of the amide NH region (lower center and enlarged in the insert). Resonances of pairs of hydrogen atoms in side chain (Asn and Gin) amide groups are indicated by horizontal lines. From Buck et al.52i...

The active site is in a cleft between a large domain with a nonpolar core and a smaller (3-sheet domain that contains many hydrogen-bonded polar side chains (Figs. 12-3,12-4). Human lysozyme has a similar structure and properties.57-59 The T4 lysozyme has an additional C-terminal domain whose function may be to bind the crosslinking peptide of the E. coli peptidoglycan. Goose lysozyme is similar in part to both hen lysozyme and T4 lysozyme. All three enzymes, as well as that of our own tears, may have evolved from a common ancestral protein.60 On the other hand, Streptomyces erythaeus has developed its own lysozyme with a completely different structure.61 An extensive series of T4 lysozyme mutants have been studied in efforts to understand protein folding and stability.61-63... 

The ROA spectra of hen lysozyme [3, 35] and bovine P-lactoglobulin [3] are shown in Fig. 7.5. These spectra contain marker bands for the secondary structural motifs discussed above showing that this information is retained... 

So, T., Ito, H., Hirata, M., Ueda, T., Imoto, T. 2001. Contribution of conformational stability of hen lysozyme to induction of type 2 T-helper immune responses. Immunology 104 259-268. 

Smith, L.J., Mark, A. E., Dobson, C.M. and Gursten, W. F. (1998) Molecular dynamic simulation of peptide fragments from hen lysozyme insight into non-native protein conformation./. Mol. Biol. 280, 703-719. 

The curves in this region cannot be classified simply as typical of mammalian lysozymes, egg lysozymes, and a-lactalbumins. The spectra for bovine, pig, and kangaroo a-lactalbumins are very similar. On the other hand, the curve for human a-lactalbumin is similar to that for human lysozyme, but different from that of domestic hen lysozyme. The curve for echidna lysozyme I resembles that of human lysozyme fairly closely. The side-chain effects of red kangaroo a-lactalbumin and echidna lysozyme I resemble those of human lysozyme (Hopper and McKenzie, 1974). 

Rawitch (1972) found a difference in rotational diffusion of these two proteins and concluded that the effective molecular volume of a-lactalbumin is greater than that of domestic hen lysozyme. 

Radford, S. E., Buck, M., Topping, K. D., Dobson, C. M. Evans, P. A. (1992a). Hydrogen exchange in native and denatured states of hen egg-white lysozyme. Proteins 14, 237-248. Radford, S. E., Dobson, C. M. Evans, P. A. (1992b). The Folding of Hen Lysozyme Involves Partially Structured Intermediates and Multiple Pathways. Nature 358, 302-307. 

Figure 3-28 A HSQC spectrum of partially denatured 129-residue hen lysozyme. Boxes enclose the tryptophan...

The 2, 3 -epoxypropyl jS-glycoside of di(N-acetyl-D-glucosamine) where R is N-acetyl glucosamine specifically inactivates hen lysozyme and several other bird lysozymes (Maron et al. 1972). The residue of hen lysozyme specifically modified by VIII is asp. 52 (Eshdat et al. 1973). X-ray analysis reveals that the two glucosamine residues of the affinity label occupy subsites B and C of the substrate binding cleft (Moult et al. 1973). The synthesis of the affinity label was accomplished by the most general procedure for the synthesis of epoxides, namely oxidation of alkenes with peroxyacids. 

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