Spectroscopic Determination of Lysozyme Conformational Changes in the Presence of Trehalose and Guanidine

Davide Barreca1, Giuseppina Laganà1, Silvana Ficarra1, Giuseppe Gattuso1, Salvatore Magazù2, R. La Torre2, Ester Tellone1, Ersilia Bellocco1
1Department of Organic and Biological Chemistry, University of Messina, Messina Italy
2Department of Physics, University of Messina, Messina, Italy

Tóm tắt

Từ khóa


Tài liệu tham khảo

Cowan, D. A. (1992). Biotechnology of the archaea. Trends in Biotechnology, 10, 315–323.

Borges, N., Ramos, A., Raven, N. D. H., Sharp, R. J., & Santos, H. (2002). Comparative study of the thermostabilizing properties of mannosylglycerate and other compatible solutes on model enzymes. Extremophiles, 6, 209–216.

Bellocco, E., Laganà, G., Barreca, D., Ficarra, S., Tellone, E., Magazù, S., et al. (2005). Role of polyols in thermal inactivation of ornithine transcarbamoylase. Physiological Research, 54(4), 395–402.

Barreca, D., Bellocco, E., Laganà, G., Leuzzi, U., Magazù, S., Migliardo, F., et al. (2008). A spectroscopic investigation of structure-breakers and structure-makers on ornithine carbamoyltransferase. Food Chemistry, 106, 1438–1442.

Bellocco, E., Barreca, D., Laganà, G., Tellone, E., Ficarra, S., Migliardo, F., et al. (2008). Influences of temperature, threshold effect of NaCl concentration on Alopias vulpinus OCT. International Journal of Biological Macromolecules, 43, 474–480. doi: 10.1016/j.ijbiomac.2008.09.008 .

Barreca, D., Bellocco, E., Galli, G., Laganà, G., Leuzzi, U., Magazù, S., et al. (2009). Stabilization effects of kosmotrope systems on ornithine carbamoyltransferase. International Journal of Biological Macromolecules, 45, 120–128.

Bellocco, E., Barreca, D., Laganà, G., Leuzzi, U., Migliardo, F., La Torre, R., et al. (2008). Neutron scattering and HPLC study on L-ascorbic acid and its degradation. Chemical Physics, 345, 191–195.

Magazù, S., Migliardo, F., Barreca, D., Bellocco, E., & Laganà, G. (2007). Aggregation processes of biomolecules in presence of trehalose. Journal of Molecular Structure, 840, 114–118.

Barreca, D., Laganà, G., Ficarra, S., Tellone, E., Leuzzi, U., Magazù, S., et al. (2010). Anti-aggregation properties of trehalose on heat-induced secondary structure and conformation changes of bovine serum albumin. Biophysical Chemistry, 147, 146–152.

Vocadlo, D. J., Davies, G. J., Laine, R., & Withers, S. G. (2001). Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate. Nature, 412, 835–838.

Hoofnagle, A. N., Resing, K. A., & Ahn, N. G. (2003). Protein analysis by hydrogen exchange mass spectrometry. Annual Reviews of Biophysics, 32, 1–25.

Busenlehner, L. S., & Armstrong, R. N. (2005). Insights into enzyme structure and dynamics elucidated by amide H/D exchange mass spectrometry. Archives of Biochemistry and Biophysics, 433, 34–46.

Batas, B., & Chandhuri, J. B. (1996). Protein refolding at high concentration using size-exclusion chromatography. Biotechnology and Bioengineering, 50, 16–23.

Beychok, S. (1966). Circular dichroism of biological macromolecules. Science, 164, 1288–1299.

Fasman, G. D., Hoving, H., & Timasheff, S. N. (1970). Circular dichroism of polypeptide and protein conformations. Film studies. Biochemistry, 9, 3316–3324.

Ellman, G. L. (1959). Tissue sulfhydryl groups. Archives of Biochememistry and Biophysics, 82, 70.

Magazù, S., Migliardo, F., & Telling, M. T. F. (2006). α,α-Trehalose/water solutions. VIII. Study of diffusive dynamics of water by high-resolution quasi elastic neutron scattering. Journal of Physical Chemistry B, 110, 1020–1025.

Magazù, S., Migliardo, F., & Ramirez-Cuesta, A. J. (2005). Inelastic neutron scattering study on bioprotectant systems. Journal of the Royal Society, Interface, 2, 527–532.

Lombardo, D. (2009). Liquid-like ordering of negatively charged poly(amidoamine) (PAMAM) dendrimers in solution. Langmuir, 25, 3271–3275.

Kiselev, M. A., Lesieur, P., Kisselev, A. M., Lombardo, D., Killany, M., & Lesieur, S. (2001). Sucrose solutions as prospective medium to study the vesicle structure: SAXS and SANS study. Journal of Alloys and Compounds, 328, 71–76.

Redfield, C., & Dobson, C. M. (1988). Sequential 1H NMR assignments and secondary structure of hen egg white lysozyme in solution. Biochemistry, 27, 122–136.

Laurents, D. V., & Baldwin, R. L. (1997). Characterization of the unfolding pathway of hen egg white lysozyme. Biochemistry, 36, 1496–1504.