Biophysical characterization of an insect lysozyme from Manduca sexta |
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Authors: | López-Zavala Alonso A de-la-Re-Vega Enrique Calderón-Arredondo Sergio A García-Orozco Karina D Velázquez Enrique F Islas-Osuna Maria A Valdez Miguel A Sotelo-Mundo Rogerio R |
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Affiliation: | Aquatic Molecular Biology, Centro de Investigación en Alimentación y Desarrollo, AC PO Box 1735, Hermosillo Sonora 83000 México. |
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Abstract: | 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. |
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