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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Biophysical characterization of an insect lysozyme from Manduca sexta.

Insect lysozyme from Manduca sexta (MS- lys) was overexpressed in E. coli and refolded to obtain active protein. Recombinant MS- lys presented a globular structure, with an alpha-helical content of 57% as assessed by circular dichroism spectroscopy. Light scattering studies showed that in solution MS- lys has a quasi-monodisperse size distribution, with a rod-like structure similar to nucleation clusters reported in egg lysozyme pre-crystallization stages. These results show that MS- lys is an excellent candidate for crystallization, folding and denaturation studies.[1]

References

  1. Biophysical characterization of an insect lysozyme from Manduca sexta. López-Zavala, A.A., de-la-Re-Vega, E., Calderón-Arredondo, S.A., García-Orozco, K.D., Velázquez, E.F., Islas-Osuna, M.A., Valdez, M.A., Sotelo-Mundo, R.R. Protein Pept. Lett. (2004) [Pubmed]
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