Analysis of the stabilization of hen lysozyme by helix macrodipole and charged side chain interaction

Journal of Biochemistry

Volumn 121, Issue 6, 1997, Pages 1076-1081

  Motoshima, Hiroyuki ^a   Mine, Shouhei ^a   Masumoto, Kiyonari ^a   Abe, Yoshito ^a   Iwashita, Hiroki ^a   Hashimoto, Yoshio ^a   Chijiiwa, Yuki ^a   Ueda, Tadashi ^a   Imoto, Taiji ^a  

^a KYUSHU UNIVERSITY   (Japan)

Author keywords

Hen lysozyme; NMR; Site directed mutagenesis; Stability; X ray crystallography

Indexed keywords

LYSOZYME; MUTANT PROTEIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; ENZYME STABILITY; ENZYME STRUCTURE; HYDROGEN BOND; MOLECULAR INTERACTION; NONHUMAN; SITE DIRECTED MUTAGENESIS;

EID: 0030760773     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021697     Document Type: Article

References (25)

1. Hol, W.G., van, Duijunen, P.T., and Berendsen, H.J. (1978) The α-helix dipole and the properties of protein. Nature 273, 443-445
2. Richardson, J.S. and Richardson, D.C. (1988) Amino acid preferences for specific locations at the ends of helices. Science 240, 1648-1652
3. Shoemaker, K.R., Kim, P.S., York, E.J., and Stewart, J.M. (1987) Tests of the helix dipole model for stabilization of α-helices. Nature 326, 563-567
4. Sali, D., Bycroft, M., and Fersht, A.R. (1988) Stabilization of protein structure by interaction of α-helix dipole with a charged side chain. Nature 335, 740-743
5. as and protein stability. Biochemistry 31, 2253-2258
6. Nicholson, H., Becktel, W.J., and Matthews, B.W. (1988) Enhanced protein thermostability from designed mutations that interact with α-helix dipoles. Nature 336, 651-656
7. Walter, S., Hubner, B., Hahn, U., and Schmid, F.X. (1995) Destabilization of a protein helix by electrostatic interaction. J. Mol. Biol. 252, 133-143
8. Hashimoto, Y., Yamada, K., Motoshima, H., Omura, T., Yamada, H., Yasukochi, T., Miki, T., Ueda, T., and Imoto, T. (1996) A mutant study of catalytic residue Asp52 in hen egg lysozyme. J. Biochem. 119, 145-150
9. a of glutamic acid-35. Biochemistry 31, 5545-5553
10. Blake, C.C.F., Koenig, D.F., Mair, G.A., North, A.C.T., Phillips, D.C., and Sarma, V.R. (1965) Structure of hen lysozyme. A three-dimensional Fourier synthesis at 2 A resolution. Nature 206, 757-761
11. Brünger, A.T. (1991) Simulated annealing in crystallography. Annu. Rev. Phys. Chem. 42, 197-223
12. Roussel, A., Fontecilla-Camps, J.C., and Cambillau, C. (1990) TURBO-FRODO: A New Program for Protein Crystallography and Modeling, Bordeaux, France: XV IUCr Congress
13. 1H NMR parameters of the common amino-acids residues measured in aqueous solution of the linear tetrapeptides H-Gly-Gly-X-Ala-OH. Biopolymers 18, 285-297
14. Bodenhauser, H., Koger, H., and Ernst, R.R. (1984) Selection of coherence-transfer pathway in NMR pulse experiments. J. Magn. Reson. 58, 370-388
15. Kumar, A., Ernst, R.R., and Wüthrich, K. (1980) A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 95, 1-6
16. 1H-NMR assignments and secondary structure of hen egg white lysozyme in solution. Biochemistry 27, 122-136
17. a of acidic residues in lysozyme. J. Biochem. 118, 946-952
18. Wishart, D.S., Sykes, B.D., and Richard, F.M. (1992) The chemical shift: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31, 1647-1651
19. Imoto, T., Forster, L.S., Rupley, J.A., and Tanaka, F. (1972) Fluorescence of lysozyme: emissions from tryptophan residues 62 and 108 and energy migration. Proc. Natl. Acad. Sci. USA 69, 1151-1155
20. Zhukovsky, E.A., Mulkerrin, M.G., and Presta, L.G. (1994) Contribution to global protein stabilization of the N-capping box in human growth hormone. Biochemistry 33, 9856-9864
21. Imoto, T., Jonson, L.N., North, A.C.T., Phillips, D.C., and Rupley, J.A. (1972) Vertebrate lysozymes in The Enzymes (Boyer, P.D., ed.) Vol. 7, 3rd ed., pp. 665-868, Academic Press, New York
22. Canfield, R.E., Kammerman, S., Sobel, J.H., and Morgan, F.J. (1971) Primary structure of lysozymes from man and goose. Nature New Biol. 232, 16-17
23. Cortopassi, G.A. and Wilson, A.C. (1990) Recent origin of the P lysozyme gene mice. Nucleic Acids Res. 18, 1191
24. Cross, M., Mangelsdorf, I., Wedel, A., and Renkawitz, R. (1988) Mouse lysozyme M gene: isolation, characterization, and expression studies. Proc. Natl. Acad. Sci. USA 85, 6232-6236
25. White, T.J., Mross, G.A., Osserman, E.F., and Wilson, A.C. (1977) Primary structure of rat lysozyme. Biochemistry 16, 1430-1436