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Biophysical Characterization Of An Insect Lysozyme From Manduca Sexta

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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 MSlys 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.

Keywords: circular dichroism; dynamic light scattering; insect; lysozyme; manduca sexta; secondary structure

Document Type: Review Article


Affiliations: Aquatic Molecular Biology , Plant Molecular Biology and Graduate Program in Sciences , Centro de Investigacion en Alimentacion y Desarrollo, A.C. P.O. Box 1735. Hermosillo Sonora 83000 Mexico,

Publication date: February 1, 2004

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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